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DnaJ homolog subfamily C member 2 (M-phase phosphoprotein 11) (Zuotin-related factor 1) [Cleaved into: DnaJ homolog subfamily C member 2, N-terminally processed]

 DNJC2_HUMAN             Reviewed;         621 AA.
Q99543; A4VCI0; Q9BVX1;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 4.
22-NOV-2017, entry version 164.
RecName: Full=DnaJ homolog subfamily C member 2;
AltName: Full=M-phase phosphoprotein 11;
AltName: Full=Zuotin-related factor 1;
Contains:
RecName: Full=DnaJ homolog subfamily C member 2, N-terminally processed;
Name=DNAJC2; Synonyms=MPHOSPH11, MPP11, ZRF1;
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 2), AND PHOSPHORYLATION.
TISSUE=Blood;
PubMed=8885239; DOI=10.1091/mbc.7.9.1455;
Matsumoto-Taniura N., Pirollet F., Monroe R., Gerace L.,
Westendorf J.M.;
"Identification of novel M phase phosphoproteins by expression
cloning.";
Mol. Biol. Cell 7:1455-1469(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[3]
PROTEIN SEQUENCE OF 2-11, CLEAVAGE OF INITIATOR METHIONINE, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Osteosarcoma;
Bienvenut W.V., Glen H., Frame M.C.;
Submitted (MAR-2008) to UniProtKB.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-621 (ISOFORM 1).
TISSUE=Cervix;
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]
TISSUE SPECIFICITY.
PubMed=11034098;
Resto V.A., Caballero O.L., Buta M.R., Westra W.H., Wu L.,
Westendorf J.M., Jen J., Hieter P., Sidransky D.;
"A putative oncogenic role for MPP11 in head and neck squamous cell
cancer.";
Cancer Res. 60:5529-5535(2000).
[6]
INDUCTION IN LEUKEMIA.
PubMed=12800198; DOI=10.1002/ijc.11200;
Greiner J., Ringhoffer M., Taniguchi M., Hauser T., Schmitt A.,
Dohner H., Schmitt M.;
"Characterization of several leukemia-associated antigens inducing
humoral immune responses in acute and chronic myeloid leukemia.";
Int. J. Cancer 106:224-231(2003).
[7]
INDUCTION IN LEUKEMIA.
PubMed=14696097; DOI=10.1002/ijc.11623;
Greiner J., Ringhoffer M., Taniguchi M., Li L., Schmitt A., Shiku H.,
Dohner H., Schmitt M.;
"mRNA expression of leukemia-associated antigens in patients with
acute myeloid leukemia for the development of specific
immunotherapies.";
Int. J. Cancer 108:704-711(2004).
[8]
FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE RAC COMPLEX, AND
INTERACTION WITH HSPA14.
PubMed=16002468; DOI=10.1073/pnas.0504400102;
Otto H., Conz C., Maier P., Wolfle T., Suzuki C.K., Jeno P.,
Rucknagel P., Stahl J., Rospert S.;
"The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-
associated complex.";
Proc. Natl. Acad. Sci. U.S.A. 102:10064-10069(2005).
[9]
FUNCTION, AND MUTAGENESIS OF 512-HIS-GLN-513.
PubMed=15802566; DOI=10.1126/science.1109247;
Hundley H.A., Walter W., Bairstow S., Craig E.A.;
"Human Mpp11 J protein: ribosome-tethered molecular chaperones are
ubiquitous.";
Science 308:1032-1034(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-49; SER-60 AND
SER-63, 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).
[11]
INDUCTION.
PubMed=17242690; DOI=10.1038/sj.cr.7310121;
Wang C., Chen X., Wang Y., Gong J., Hu G.;
"C/EBPalphap30 plays transcriptional regulatory roles distinct from
C/EBPalphap42.";
Cell Res. 17:374-383(2007).
[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-47, AND 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).
[14]
EPITOPE REGION.
PubMed=20231810;
Al Qudaihi G., Lehe C., Dickinson A., Eltayeb K., Rasheed W.,
Chaudhri N., Aljurf M., Dermime S.;
"Identification of a novel peptide derived from the M-phase
phosphoprotein 11 (MPP11) leukemic antigen recognized by human CD8+
cytotoxic T lymphocytes.";
Hematol. Oncol. Stem Cell Ther. 3:24-33(2010).
[15]
FUNCTION AS CHROMATIN REGULATOR, SUBCELLULAR LOCATION,
UBIQUITIN-BINDING, AND DOMAIN ZRF1-UBD.
PubMed=21179169; DOI=10.1038/nature09574;
Richly H., Rocha-Viegas L., Ribeiro J.D., Demajo S., Gundem G.,
Lopez-Bigas N., Nakagawa T., Rospert S., Ito T., Di Croce L.;
"Transcriptional activation of polycomb-repressed genes by ZRF1.";
Nature 468:1124-1128(2010).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-49, 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).
[17]
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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND 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).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-49, 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).
-!- FUNCTION: Acts both as a chaperone in the cytosol and as a
chromatin regulator in the nucleus. When cytosolic, acts as a
molecular chaperone: component of the ribosome-associated complex
(RAC), a complex involved in folding or maintaining nascent
polypeptides in a folding-competent state. In the RAC complex,
stimulates the ATPase activity of the ribosome-associated pool of
Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide
chain. When nuclear, mediates the switching from polycomb-
repressed genes to an active state: specifically recruited at
histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes
the displacement of the polycomb PRC1 complex from chromatin,
thereby facilitating transcription activation. Specifically binds
DNA sequence 5'-GTCAAGC-3'. {ECO:0000269|PubMed:15802566,
ECO:0000269|PubMed:16002468, ECO:0000269|PubMed:21179169}.
-!- SUBUNIT: Interacts (via ZRF1-UBD region) with ID1 (By similarity).
Component of ribosome-associated complex (RAC), a heterodimer
composed of Hsp70/DnaK-type chaperone HSPA14 and Hsp40/DnaJ-type
chaperone DNAJC2. {ECO:0000250, ECO:0000269|PubMed:16002468}.
-!- INTERACTION:
P0C0S8:HIST1H2AM; NbExp=2; IntAct=EBI-11017224, EBI-1390628;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21179169}.
Cytoplasm, cytosol {ECO:0000269|PubMed:16002468,
ECO:0000269|PubMed:21179169}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q99543-1; Sequence=Displayed;
Name=2;
IsoId=Q99543-2; Sequence=VSP_023562;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:11034098}.
-!- INDUCTION: Expression is repressed by CEBPA. Strongly
overexpressed in leukemic cells. {ECO:0000269|PubMed:12800198,
ECO:0000269|PubMed:14696097, ECO:0000269|PubMed:17242690}.
-!- DOMAIN: The ZRF1-UBD region specifically recognizes and binds
H2AK119ub. The ZRF1-UBD region is also involved in protein-protein
interactions with other proteins, suggesting that it may be masked
by some regulator, thereby preventing its association with
H2AK119ub. {ECO:0000269|PubMed:21179169}.
-!- PTM: Phosphorylated in M (mitotic) phase.
{ECO:0000269|PubMed:8885239}.
-!- MISCELLANEOUS: Constitutes a myeloid leukemia-associated antigen
and might be a target for leukemia T-cell therapy.
-!- SEQUENCE CAUTION:
Sequence=AAI39752.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAA66913.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; X98260; CAA66913.1; ALT_INIT; mRNA.
EMBL; AC004668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000859; AAH00859.1; -; mRNA.
EMBL; BC139751; AAI39752.1; ALT_INIT; mRNA.
CCDS; CCDS43628.1; -. [Q99543-1]
CCDS; CCDS47679.1; -. [Q99543-2]
RefSeq; NP_001123359.1; NM_001129887.1. [Q99543-2]
RefSeq; NP_055192.1; NM_014377.1. [Q99543-1]
UniGene; Hs.558476; -.
PDB; 2M2E; NMR; -; A=551-621.
PDBsum; 2M2E; -.
ProteinModelPortal; Q99543; -.
SMR; Q99543; -.
BioGrid; 117946; 20.
DIP; DIP-60462N; -.
IntAct; Q99543; 5.
STRING; 9606.ENSP00000368565; -.
iPTMnet; Q99543; -.
PhosphoSitePlus; Q99543; -.
BioMuta; DNAJC2; -.
DMDM; 296439472; -.
EPD; Q99543; -.
MaxQB; Q99543; -.
PaxDb; Q99543; -.
PeptideAtlas; Q99543; -.
PRIDE; Q99543; -.
DNASU; 27000; -.
Ensembl; ENST00000249270; ENSP00000249270; ENSG00000105821. [Q99543-2]
Ensembl; ENST00000379263; ENSP00000368565; ENSG00000105821. [Q99543-1]
GeneID; 27000; -.
KEGG; hsa:27000; -.
UCSC; uc003vbo.4; human. [Q99543-1]
CTD; 27000; -.
DisGeNET; 27000; -.
EuPathDB; HostDB:ENSG00000105821.14; -.
GeneCards; DNAJC2; -.
HGNC; HGNC:13192; DNAJC2.
HPA; HPA020454; -.
MIM; 605502; gene.
neXtProt; NX_Q99543; -.
OpenTargets; ENSG00000105821; -.
PharmGKB; PA162383835; -.
eggNOG; KOG0724; Eukaryota.
eggNOG; COG5269; LUCA.
GeneTree; ENSGT00530000063419; -.
HOGENOM; HOG000006900; -.
HOVERGEN; HBG008782; -.
InParanoid; Q99543; -.
KO; K09522; -.
OMA; TTPDRWD; -.
OrthoDB; EOG091G04S8; -.
PhylomeDB; Q99543; -.
TreeFam; TF105834; -.
Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
GeneWiki; ZRF1; -.
GenomeRNAi; 27000; -.
PRO; PR:Q99543; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000105821; -.
CleanEx; HS_DNAJC2; -.
ExpressionAtlas; Q99543; baseline and differential.
Genevisible; Q99543; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0001671; F:ATPase activator activity; TAS:Reactome.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0042393; F:histone binding; IDA:UniProtKB.
GO; GO:0030544; F:Hsp70 protein binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0061649; F:ubiquitin modification-dependent histone binding; IDA:UniProtKB.
GO; GO:0051083; P:'de novo' cotranslational protein folding; TAS:UniProtKB.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0006260; P:DNA replication; IEA:Ensembl.
GO; GO:2000279; P:negative regulation of DNA biosynthetic process; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd06257; DnaJ; 1.
CDD; cd00167; SANT; 2.
Gene3D; 1.10.287.110; -; 1.
InterPro; IPR036869; DnaJ_dom_sf.
InterPro; IPR001623; DnaJ_domain.
InterPro; IPR018253; DnaJ_domain_CS.
InterPro; IPR009057; Homeobox-like_sf.
InterPro; IPR032003; RAC_head.
InterPro; IPR001005; SANT/Myb.
InterPro; IPR017884; SANT_dom.
Pfam; PF00226; DnaJ; 1.
Pfam; PF00249; Myb_DNA-binding; 2.
Pfam; PF16717; RAC_head; 1.
SMART; SM00271; DnaJ; 1.
SMART; SM00717; SANT; 2.
SUPFAM; SSF46565; SSF46565; 1.
SUPFAM; SSF46689; SSF46689; 2.
PROSITE; PS00636; DNAJ_1; 1.
PROSITE; PS50076; DNAJ_2; 1.
PROSITE; PS51293; SANT; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing; Chaperone;
Chromatin regulator; Complete proteome; Cytoplasm;
Direct protein sequencing; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Transcription; Transcription regulation.
CHAIN 1 621 DnaJ homolog subfamily C member 2.
/FTId=PRO_0000425752.
INIT_MET 1 1 Removed; alternate. {ECO:0000269|Ref.3}.
CHAIN 2 621 DnaJ homolog subfamily C member 2, N-
terminally processed.
/FTId=PRO_0000071123.
DOMAIN 88 161 J. {ECO:0000255|PROSITE-
ProRule:PRU00286}.
DOMAIN 449 511 SANT 1. {ECO:0000255|PROSITE-
ProRule:PRU00624}.
DOMAIN 549 604 SANT 2. {ECO:0000255|PROSITE-
ProRule:PRU00624}.
REGION 23 31 Epitope (recognized by CD8(+) cytotoxic
T-lymphocytes).
REGION 160 250 ZRF1-UBD.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 47 47 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 49 49 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 60 60 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 63 63 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
VAR_SEQ 362 414 Missing (in isoform 2).
{ECO:0000303|PubMed:8885239}.
/FTId=VSP_023562.
MUTAGEN 512 513 HQ->AA: Loss of function.
{ECO:0000269|PubMed:15802566}.
CONFLICT 252 252 R -> G (in Ref. 1; CAA66913).
{ECO:0000305}.
CONFLICT 472 472 G -> R (in Ref. 1; CAA66913).
{ECO:0000305}.
CONFLICT 578 578 E -> K (in Ref. 4; AAI39752).
{ECO:0000305}.
HELIX 556 568 {ECO:0000244|PDB:2M2E}.
HELIX 576 583 {ECO:0000244|PDB:2M2E}.
HELIX 589 618 {ECO:0000244|PDB:2M2E}.
SEQUENCE 621 AA; 71996 MW; E4DAEE7A73D0F64C CRC64;
MLLLPSAADG RGTAITHALT SASTLCQVEP VGRWFEAFVK RRNRNASASF QELEDKKELS
EESEDEELQL EEFPMLKTLD PKDWKNQDHY AVLGLGHVRY KATQRQIKAA HKAMVLKHHP
DKRKAAGEPI KEGDNDYFTC ITKAYEMLSD PVKRRAFNSV DPTFDNSVPS KSEAKDNFFE
VFTPVFERNS RWSNKKNVPK LGDMNSSFED VDIFYSFWYN FDSWREFSYL DEEEKEKAEC
RDERRWIEKQ NRATRAQRKK EEMNRIRTLV DNAYSCDPRI KKFKEEEKAK KEAEKKAKAE
AKRKEQEAKE KQRQAELEAA RLAKEKEEEE VRQQALLAKK EKDIQKKAIK KERQKLRNSC
KTWNHFSDNE AERVKMMEEV EKLCDRLELA SLQCLNETLT SCTKEVGKAA LEKQIEEINE
QIRKEKEEAE ARMRQASKNT EKSTGGGGNG SKNWSEDDLQ LLIKAVNLFP AGTNSRWEVI
ANYMNIHSSS GVKRTAKDVI GKAKSLQKLD PHQKDDINKK AFDKFKKEHG VVPQADNATP
SERFEGPYTD FTPWTTEEQK LLEQALKTYP VNTPERWEKI AEAVPGRTKK DCMKRYKELV
EMVKAKKAAQ EQVLNASRAK K


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EIAAB11569 DnaJ homolog subfamily C member 2,Dnajc2,MIDA1,Mida1,Mouse,Mouse Id associate 1,Mus musculus,Zrf1,Zuotin-related factor 1
EIAAB11300 ABBP-2,APOBEC1-binding protein 2,DnaJ homolog subfamily B member 11,DnaJ protein homolog 9,DNAJB11,EDJ,ER-associated DNAJ,ER-associated dnaJ protein 3,ER-associated Hsp40 co-chaperone,ERdj3,ERJ3,ERj3p
EIAAB11297 DnaJ homolog subfamily B member 11,Dnajb11,ER-associated DNAJ,ER-associated dnaJ protein 3,ER-associated Hsp40 co-chaperone,ERdj3,ERj3p,Liver regeneration-related protein LRRGT00084,Rat,Rattus norvegi
EIAAB11301 Bos taurus,Bovine,DnaJ homolog subfamily B member 11,DNAJB11,ER-associated DNAJ,ER-associated dnaJ protein 3,ER-associated Hsp40 co-chaperone,ERdj3,ERj3p
EIAAB11564 DnaJ homolog subfamily C member 1,DnaJ protein homolog MTJ1,DNAJC1,Homo sapiens,HTJ1,Human
EIAAB11298 ABBP-2,APOBEC1-binding protein 2,DnaJ homolog subfamily B member 11,Dnajb11,ER-associated DNAJ,ER-associated dnaJ protein 3,ER-associated Hsp40 co-chaperone,ERdj3,ERj3p,Mouse,Mus musculus
EIAAB11351 Bos taurus,Bovine,DnaJ homolog subfamily C member 27,DNAJC27,Rab and DnaJ domain-containing protein,RBJ
EIAAB11353 DnaJ homolog subfamily C member 27,Dnajc27,Rab and DnaJ domain-containing protein,Rat,Rattus norvegicus,Rbj
EIAAB11543 DnaJ homolog subfamily B member 3,DnaJ protein homolog 3,Dnajb3,Heat shock protein J3,Hsj3,HSJ-3,Mouse,Msj1,MSJ-1,Mus musculus
EIAAB11538 DnaJ homolog subfamily A member 3, mitochondrial,DnaJ protein Tid-1,Dnaja3,Mouse,mTid-1,Mus musculus,Tid1,Tumorous imaginal discs protein Tid56 homolog
EIAAB11586 DnaJ homolog subfamily C member 9,DnaJ protein SB73,DNAJC9,Homo sapiens,Human
EIAAB11350 DnaJ homolog subfamily C member 27,Dnajc27,Mouse,Mus musculus,Rab and DnaJ domain-containing protein,Rabj,Rbj
EIAAB11565 DnaJ homolog subfamily C member 1,DnaJ protein homolog MTJ1,Dnajc1,Dnajl1,Mouse,Mtj1,Mus musculus
EIAAB11352 DnaJ homolog subfamily C member 27,DNAJC27,Homo sapiens,Human,Rab and DnaJ domain-containing protein,RABJS,RBJ
EIAAB11323 DnaJ homolog subfamily C member 14,DnaJ protein homolog 3,DNAJC14,Dopamine receptor-interacting protein of 78 kDa,DRIP78,DRIP78,HDJ3,hDj-3,Homo sapiens,Human,Human DnaJ protein 3
EIAAB11299 Canis familiaris,Canis lupus familiaris,DnaJ homolog subfamily B member 11,DNAJB11,Dog,ER-associated DNAJ,ER-associated dnaJ protein 3,ER-associated Hsp40 co-chaperone,ERdj3,ERj3p
EIAAB11563 Canis familiaris,Canis lupus familiaris,DnaJ homolog subfamily C member 1,DnaJ protein homolog MTJ1,DNAJC1,Dog
EIAAB11349 Chicken,DnaJ homolog subfamily C member 27,DNAJC27,Gallus gallus,Rab and DnaJ domain-containing protein,RBJ
EIAAB11532 DnaJ homolog subfamily A member 1,Dnaja1,DnaJ-like protein 1,Heat shock protein J2,Hsj2,HSJ-2,Rat,Rattus norvegicus,Rdj1
EIAAB11547 DnaJ homolog subfamily B member 4,DNAJB4,DNAJW,Heat shock 40 kDa protein 1 homolog,Heat shock protein 40 homolog,HLJ1,Homo sapiens,HSP40 homolog,Human,Human liver DnaJ-like protein


 

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