GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

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

DnaJ homolog subfamily B member 11 (APOBEC1-binding protein 2) (ABBP-2) (DnaJ protein homolog 9) (ER-associated DNAJ) (ER-associated Hsp40 co-chaperone) (Endoplasmic reticulum DNA J domain-containing protein 3) (ER-resident protein ERdj3) (ERdj3) (ERj3p) (HEDJ) (Human DnaJ protein 9) (hDj-9) (PWP1-interacting protein 4)

 DJB11_HUMAN             Reviewed;         358 AA.
Q9UBS4; Q542Y5; Q542Y9; Q6IAQ8; Q96JC6;
18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
08-MAY-2019, entry version 178.
RecName: Full=DnaJ homolog subfamily B member 11;
AltName: Full=APOBEC1-binding protein 2;
Short=ABBP-2;
AltName: Full=DnaJ protein homolog 9;
AltName: Full=ER-associated DNAJ;
AltName: Full=ER-associated Hsp40 co-chaperone;
AltName: Full=Endoplasmic reticulum DNA J domain-containing protein 3;
Short=ER-resident protein ERdj3;
Short=ERdj3;
Short=ERj3p;
AltName: Full=HEDJ;
AltName: Full=Human DnaJ protein 9;
Short=hDj-9;
AltName: Full=PWP1-interacting protein 4;
Flags: Precursor;
Name=DNAJB11; Synonyms=EDJ, ERJ3, HDJ9;
ORFNames=PSEC0121, UNQ537/PRO1080;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11147971; DOI=10.1379/1466-1268(2000)005<0098:MHDHCO>2.0.CO;2;
Ohtsuka K., Hata M.;
"Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal
for their classification and nomenclature.";
Cell Stress Chaperones 5:98-112(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION,
INTERACTION WITH HSPA5, TISSUE SPECIFICITY, AND GLYCOSYLATION.
TISSUE=Skeletal muscle;
PubMed=10827079; DOI=10.1074/jbc.M000739200;
Yu M., Haslam R.H.A., Haslam D.B.;
"HEDJ, an Hsp40 co-chaperone localized to the endoplasmic reticulum of
human cells.";
J. Biol. Chem. 275:24984-24992(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND GLYCOSYLATION.
TISSUE=Placenta;
PubMed=15195998; DOI=10.1515/BC.2004.043;
Bies C., Blum R., Dudek J., Nastainczyk W., Oberhauser S., Jung M.,
Zimmermann R.;
"Characterization of pancreatic ERj3p, a homolog of yeast DnaJ-like
protein Scj1p.";
Biol. Chem. 385:389-395(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-264.
TISSUE=Tonsil;
Honore B.;
"hPWP1-interacting protein 4.";
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-264.
TISSUE=Placenta, and Retinoblastoma;
PubMed=16303743; DOI=10.1093/dnares/12.2.117;
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
Isogai T.;
"Signal sequence and keyword trap in silico for selection of full-
length human cDNAs encoding secretion or membrane proteins from oligo-
capped cDNA libraries.";
DNA Res. 12:117-126(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[9]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
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).
[11]
TISSUE SPECIFICITY.
PubMed=11584023; DOI=10.1074/jbc.M109215200;
Lau P.P., Villanueva H., Kobayashi K., Nakamuta M., Chang B.H.-J.,
Chan L.;
"A DnaJ protein, apobec-1-binding protein-2, modulates apolipoprotein
B mRNA editing.";
J. Biol. Chem. 276:46445-46452(2001).
[12]
COMPONENT OF A CHAPERONE COMPLEX.
PubMed=12475965; DOI=10.1091/mbc.E02-05-0311;
Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
"A subset of chaperones and folding enzymes form multiprotein
complexes in endoplasmic reticulum to bind nascent proteins.";
Mol. Biol. Cell 13:4456-4469(2002).
[13]
SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=15544163; DOI=10.1379/CSC-52.1;
Nakanishi K., Kamiguchi K., Torigoe T., Nabeta C., Hirohashi Y.,
Asanuma H., Tobioka H., Koge N., Harada O., Tamura Y., Nagano H.,
Yano S., Chiba S., Matsumoto H., Sato N.;
"Localization and function in endoplasmic reticulum stress tolerance
of ERdj3, a new member of Hsp40 family protein.";
Cell Stress Chaperones 9:253-264(2004).
[14]
FUNCTION, SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY,
GLYCOSYLATION, INTERACTION WITH DENATURED SUBSTRATES, AND MUTAGENESIS
OF HIS-53.
PubMed=15525676; DOI=10.1091/mbc.E04-05-0434;
Shen Y., Hendershot L.M.;
"ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue,
serves as a cofactor for BiP's interactions with unfolded
substrates.";
Mol. Biol. Cell 16:40-50(2005).
[15]
MUTAGENESIS OF CYS-169; CYS-171; CYS-193 AND CYS-196, AND INTERACTION
WITH DENATURED SUBSTRATES.
PubMed=17976514; DOI=10.1016/j.abb.2007.10.001;
Marcus N.Y., Marcus R.A., Schmidt B.Z., Haslam D.B.;
"Contribution of the HEDJ/ERdj3 cysteine-rich domain to substrate
interactions.";
Arch. Biochem. Biophys. 468:147-158(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-188, AND 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).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-261.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[18]
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).
[19]
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).
[20]
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).
[21]
FUNCTION, INVOLVEMENT IN PKD6, AND VARIANTS PKD6 ARG-54; PRO-77 AND
206-ARG--TYR-358 DEL.
PubMed=29706351; DOI=10.1016/j.ajhg.2018.03.013;
Genkyst Study Group;
HALT Progression of Polycystic Kidney Disease Group;
Consortium for Radiologic Imaging Studies of Polycystic Kidney Disease;
Cornec-Le Gall E., Olson R.J., Besse W., Heyer C.M., Gainullin V.G.,
Smith J.M., Audrezet M.P., Hopp K., Porath B., Shi B., Baheti S.,
Senum S.R., Arroyo J., Madsen C.D., Ferec C., Joly D., Jouret F.,
Fikri-Benbrahim O., Charasse C., Coulibaly J.M., Yu A.S., Khalili K.,
Pei Y., Somlo S., Le Meur Y., Torres V.E., Harris P.C.;
"Monoallelic mutations to DNAJB11 cause atypical autosomal-dominant
polycystic kidney disease.";
Am. J. Hum. Genet. 102:832-844(2018).
-!- FUNCTION: As a co-chaperone for HSPA5 it is required for proper
folding, trafficking or degradation of proteins (PubMed:10827079,
PubMed:15525676, PubMed:29706351). Binds directly to both unfolded
proteins that are substrates for ERAD and nascent unfolded peptide
chains, but dissociates from the HSPA5-unfolded protein complex
before folding is completed (PubMed:15525676). May help recruiting
HSPA5 and other chaperones to the substrate. Stimulates HSPA5
ATPase activity (PubMed:10827079). It is necessary for maturation
and correct trafficking of PKD1 (PubMed:29706351).
{ECO:0000269|PubMed:10827079, ECO:0000269|PubMed:15525676,
ECO:0000269|PubMed:29706351}.
-!- SUBUNIT: Part of a large chaperone multiprotein complex comprising
DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1,
UGT1A1 and very small amounts of ERP29, but not, or at very low
levels, CALR nor CANX. Binds to denatured substrates in an ATP-
independent manner. Interacts via the J domain with HSPA5 in an
ATP-dependent manner. {ECO:0000269|PubMed:10827079,
ECO:0000269|PubMed:15525676, ECO:0000269|PubMed:17976514}.
-!- INTERACTION:
P11021:HSPA5; NbExp=3; IntAct=EBI-713113, EBI-354921;
Q8ZQQ2:slrP (xeno); NbExp=4; IntAct=EBI-713113, EBI-10712653;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
{ECO:0000269|PubMed:10827079, ECO:0000269|PubMed:15195998,
ECO:0000269|PubMed:15525676, ECO:0000269|PubMed:15544163}.
Note=Associated with the ER membrane in a C-terminally epitope-
tagged construct.
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:10827079, ECO:0000269|PubMed:11584023,
ECO:0000269|PubMed:15525676}.
-!- INDUCTION: By endoplasmic reticulum stress-inducing agents such as
thapsigargin and tunicamycin. {ECO:0000269|PubMed:15525676,
ECO:0000269|PubMed:15544163}.
-!- PTM: Contains high-mannose Endo H-sensitive carbohydrates.
-!- PTM: Cys-169, Cys-171, Cys-193 and Cys-196 form intramolecular
disulfide bonds. The preferential partner for each Cys is not
known.
-!- PTM: Thr-188 was reported to be phosphorylated upon DNA damage by
ATM or ATR; however as this position has been shown to be in the
ER lumen, the in vivo relevance is not proven.
-!- DISEASE: Polycystic kidney disease 6 with or without polycystic
liver disease (PKD6) [MIM:618061]: A form of polycystic kidney
disease, a disorder characterized by progressive formation and
enlargement of cysts in both kidneys, typically leading to end-
stage renal disease in adult life. Cysts also occur in other
organs, particularly the liver. PKD6 inheritance is autosomal
dominant. {ECO:0000269|PubMed:29706351}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- CAUTION: PubMed:11584023 reported a cytosolic, as well as nuclear
subcellular location. This result was obtained using an N-
terminally GFP-tagged construct which most probably affected
signal peptide-driven targeting to the ER. As a consequence, the
in vivo revelance of the observed interaction with APOBEC1, a
nuclear protein, is dubious. This holds true for the interaction
with PWP1. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AB028859; BAA88307.1; -; mRNA.
EMBL; AF228505; AAF61711.1; -; mRNA.
EMBL; AJ250137; CAB65118.1; -; mRNA.
EMBL; AF277317; AAK69110.1; -; mRNA.
EMBL; AY359043; AAQ89402.1; -; mRNA.
EMBL; AK075300; BAC11533.1; -; mRNA.
EMBL; AK075430; BAC11617.1; -; mRNA.
EMBL; BT007063; AAP35712.1; -; mRNA.
EMBL; CR457096; CAG33377.1; -; mRNA.
EMBL; CH471052; EAW78190.1; -; Genomic_DNA.
EMBL; BC001144; AAH01144.1; -; mRNA.
CCDS; CCDS3277.1; -.
PIR; T52073; T52073.
RefSeq; NP_057390.1; NM_016306.5.
SMR; Q9UBS4; -.
BioGrid; 119699; 98.
DIP; DIP-29678N; -.
IntAct; Q9UBS4; 62.
MINT; Q9UBS4; -.
STRING; 9606.ENSP00000414398; -.
GlyConnect; 1185; -.
iPTMnet; Q9UBS4; -.
PhosphoSitePlus; Q9UBS4; -.
BioMuta; DNAJB11; -.
DMDM; 18203497; -.
OGP; Q9UBS4; -.
REPRODUCTION-2DPAGE; IPI00008454; -.
EPD; Q9UBS4; -.
jPOST; Q9UBS4; -.
MaxQB; Q9UBS4; -.
PaxDb; Q9UBS4; -.
PeptideAtlas; Q9UBS4; -.
PRIDE; Q9UBS4; -.
ProteomicsDB; 84046; -.
TopDownProteomics; Q9UBS4; -.
DNASU; 51726; -.
Ensembl; ENST00000265028; ENSP00000265028; ENSG00000090520.
Ensembl; ENST00000439351; ENSP00000414398; ENSG00000090520.
GeneID; 51726; -.
KEGG; hsa:51726; -.
UCSC; uc003fqi.4; human.
CTD; 51726; -.
DisGeNET; 51726; -.
GeneCards; DNAJB11; -.
GeneReviews; DNAJB11; -.
HGNC; HGNC:14889; DNAJB11.
HPA; HPA010814; -.
HPA; HPA017051; -.
MIM; 611341; gene.
MIM; 618061; phenotype.
neXtProt; NX_Q9UBS4; -.
OpenTargets; ENSG00000090520; -.
PharmGKB; PA27413; -.
eggNOG; KOG0713; Eukaryota.
eggNOG; COG0484; LUCA.
GeneTree; ENSGT00940000155792; -.
HOGENOM; HOG000226718; -.
InParanoid; Q9UBS4; -.
KO; K09517; -.
OMA; KEGMMDH; -.
OrthoDB; 687505at2759; -.
PhylomeDB; Q9UBS4; -.
TreeFam; TF105144; -.
Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
ChiTaRS; DNAJB11; human.
GeneWiki; DNAJB11; -.
GenomeRNAi; 51726; -.
PRO; PR:Q9UBS4; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000090520; Expressed in 200 organ(s), highest expression level in tendon of biceps brachii.
Genevisible; Q9UBS4; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:AgBase.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
GO; GO:0036498; P:IRE1-mediated unfolded protein response; TAS:Reactome.
GO; GO:0032781; P:positive regulation of ATPase activity; IDA:AgBase.
GO; GO:0006457; P:protein folding; IEA:InterPro.
GO; GO:0051604; P:protein maturation; IMP:UniProtKB.
CDD; cd06257; DnaJ; 1.
Gene3D; 1.10.287.110; -; 1.
InterPro; IPR002939; DnaJ_C.
InterPro; IPR001623; DnaJ_domain.
InterPro; IPR018253; DnaJ_domain_CS.
InterPro; IPR008971; HSP40/DnaJ_pept-bd.
InterPro; IPR036869; J_dom_sf.
Pfam; PF00226; DnaJ; 1.
Pfam; PF01556; DnaJ_C; 1.
PRINTS; PR00625; JDOMAIN.
SMART; SM00271; DnaJ; 1.
SUPFAM; SSF46565; SSF46565; 1.
SUPFAM; SSF49493; SSF49493; 2.
PROSITE; PS00636; DNAJ_1; 1.
PROSITE; PS50076; DNAJ_2; 1.
1: Evidence at protein level;
Chaperone; Complete proteome; Disease mutation; Disulfide bond;
Endoplasmic reticulum; Glycoprotein; Phosphoprotein; Polymorphism;
Reference proteome; Signal.
SIGNAL 1 22 {ECO:0000250}.
CHAIN 23 358 DnaJ homolog subfamily B member 11.
/FTId=PRO_0000007260.
DOMAIN 25 90 J. {ECO:0000255|PROSITE-
ProRule:PRU00286}.
MOD_RES 188 188 Phosphothreonine.
{ECO:0000244|PubMed:17525332}.
CARBOHYD 261 261 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
VARIANT 54 54 P -> R (in PKD6).
{ECO:0000269|PubMed:29706351}.
/FTId=VAR_081002.
VARIANT 77 77 L -> P (in PKD6).
{ECO:0000269|PubMed:29706351}.
/FTId=VAR_081003.
VARIANT 206 358 Missing (in PKD6).
{ECO:0000269|PubMed:29706351}.
/FTId=VAR_081004.
VARIANT 264 264 I -> V (in dbSNP:rs8147).
{ECO:0000269|PubMed:16303743,
ECO:0000269|Ref.4}.
/FTId=VAR_016092.
MUTAGEN 53 53 H->Q: Loss of HSPA5-binding, but no
effect on interaction with denatured
substrates.
{ECO:0000269|PubMed:15525676}.
MUTAGEN 169 169 C->S: Drastic loss of interaction with
denatured substrates.
{ECO:0000269|PubMed:17976514}.
MUTAGEN 171 171 C->S: Drastic loss of interaction with
denatured substrates.
{ECO:0000269|PubMed:17976514}.
MUTAGEN 193 193 C->S: Drastic loss of interaction with
denatured substrates.
{ECO:0000269|PubMed:17976514}.
MUTAGEN 196 196 C->S: Drastic loss of interaction with
denatured substrates.
{ECO:0000269|PubMed:17976514}.
CONFLICT 247 247 K -> R (in Ref. 8; CAG33377).
{ECO:0000305}.
SEQUENCE 358 AA; 40514 MW; 580CC4D66A06B734 CRC64;
MAPQNLSTFC LLLLYLIGAV IAGRDFYKIL GVPRSASIKD IKKAYRKLAL QLHPDRNPDD
PQAQEKFQDL GAAYEVLSDS EKRKQYDTYG EEGLKDGHQS SHGDIFSHFF GDFGFMFGGT
PRQQDRNIPR GSDIIVDLEV TLEEVYAGNF VEVVRNKPVA RQAPGKRKCN CRQEMRTTQL
GPGRFQMTQE VVCDECPNVK LVNEERTLEV EIEPGVRDGM EYPFIGEGEP HVDGEPGDLR
FRIKVVKHPI FERRGDDLYT NVTISLVESL VGFEMDITHL DGHKVHISRD KITRPGAKLW
KKGEGLPNFD NNNIKGSLII TFDVDFPKEQ LTEEAREGIK QLLKQGSVQK VYNGLQGY


Related products :

Catalog number Product name Quantity
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
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
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
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
EIAAB11310 DnaJ homolog subfamily C member 10,Dnajc10,Endoplasmic reticulum DnaJ-PDI fusion protein 1,Erdj5,ER-resident protein ERdj5,J domain-containing PDI-like protein,J domain-containing protein disulfide is
U0872h CLIA DnaJ homolog subfamily B member 1,DnaJ protein homolog 1,DNAJ1,DNAJB1,HDJ1,hDj-1,Heat shock 40 kDa protein 1,Heat shock protein 40,Homo sapiens,HSP40,HSPF1,Human,Human DnaJ protein 1 96T
E0872h ELISA DnaJ homolog subfamily B member 1,DnaJ protein homolog 1,DNAJ1,DNAJB1,HDJ1,hDj-1,Heat shock 40 kDa protein 1,Heat shock protein 40,Homo sapiens,HSP40,HSPF1,Human,Human DnaJ protein 1 96T
E0872h ELISA kit DnaJ homolog subfamily B member 1,DnaJ protein homolog 1,DNAJ1,DNAJB1,HDJ1,hDj-1,Heat shock 40 kDa protein 1,Heat shock protein 40,Homo sapiens,HSP40,HSPF1,Human,Human DnaJ protein 1 96T
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
EIAAB11531 DnaJ homolog subfamily A member 1,DnaJ protein homolog 2,DNAJ2,DNAJA1,HDJ2,hDj-2,Heat shock 40 kDa protein 4,Heat shock protein J2,Homo sapiens,HSDJ,HSJ2,HSJ-2,HSPF4,Human,Human DnaJ protein 2
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
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
EIAAB11352 DnaJ homolog subfamily C member 27,DNAJC27,Homo sapiens,Human,Rab and DnaJ domain-containing protein,RABJS,RBJ
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
EIAAB11353 DnaJ homolog subfamily C member 27,Dnajc27,Rab and DnaJ domain-containing protein,Rat,Rattus norvegicus,Rbj
EIAAB11351 Bos taurus,Bovine,DnaJ homolog subfamily C member 27,DNAJC27,Rab and DnaJ domain-containing protein,RBJ
EIAAB11350 DnaJ homolog subfamily C member 27,Dnajc27,Mouse,Mus musculus,Rab and DnaJ domain-containing protein,Rabj,Rbj
EIAAB11532 DnaJ homolog subfamily A member 1,Dnaja1,DnaJ-like protein 1,Heat shock protein J2,Hsj2,HSJ-2,Rat,Rattus norvegicus,Rdj1
EIAAB11564 DnaJ homolog subfamily C member 1,DnaJ protein homolog MTJ1,DNAJC1,Homo sapiens,HTJ1,Human
EIAAB11542 DnaJ homolog subfamily B member 2,DnaJ protein homolog 1,DNAJB2,Heat shock 40 kDa protein 3,Heat shock protein J1,Homo sapiens,HSJ1,HSJ-1,HSPF3,Human
EIAAB11537 DnaJ homolog subfamily A member 3, mitochondrial,DnaJ protein Tid-1,DNAJA3,HCA57,Hepatocellular carcinoma-associated antigen 57,Homo sapiens,hTid-1,Human,TID1,Tumorous imaginal discs protein Tid56 hom
10-782-55040 DnaJ homolog subfamily B member 1 - Heat shock 40 kDa protein 1; Heat shock protein 40; HSP40; DnaJ protein homolog 1; HDJ-1 N_A 0.05 mg
10-782-55040 DnaJ homolog subfamily B member 1 - Heat shock 40 kDa protein 1; Heat shock protein 40; HSP40; DnaJ protein homolog 1; HDJ-1 N_A 0.2 mg
EIAAB11586 DnaJ homolog subfamily C member 9,DnaJ protein SB73,DNAJC9,Homo sapiens,Human

Kits Elisa; taq POLYMERASE

Search in Google:

google

Share this page:
share on twitter rss feedsfacebookgoogle gentaur



Quick order!
Enter catalog number :


Gentaur; yes we can

Pathways :
WP1531: Vitamin D synthesis
WP1616: ABC transporters
WP1689: Porphyrin and chlorophyll metabolism
WP2199: Seed Development
WP2292: Chemokine signaling pathway
WP731: Sterol regulatory element binding protein related
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair

Related Genes :
[DNAJB11 EDJ ERJ3 HDJ9 PSEC0121 UNQ537/PRO1080] DnaJ homolog subfamily B member 11 (APOBEC1-binding protein 2) (ABBP-2) (DnaJ protein homolog 9) (ER-associated DNAJ) (ER-associated Hsp40 co-chaperone) (Endoplasmic reticulum DNA J domain-containing protein 3) (ER-resident protein ERdj3) (ERdj3) (ERj3p) (HEDJ) (Human DnaJ protein 9) (hDj-9) (PWP1-interacting protein 4)
[Dnajb11] DnaJ homolog subfamily B member 11 (APOBEC1-binding protein 2) (ABBP-2) (ER-associated DNAJ) (ER-associated Hsp40 co-chaperone) (Endoplasmic reticulum DNA J domain-containing protein 3) (ER-resident protein ERdj3) (ERdj3) (ERj3p)
[Dnajb11] DnaJ homolog subfamily B member 11 (ER-associated DNAJ) (ER-associated Hsp40 co-chaperone) (Endoplasmic reticulum DNA J domain-containing protein 3) (ER-resident protein ERdj3) (ERdj3) (ERj3p) (Liver regeneration-related protein LRRGT00084)
[Dnajc10 Erdj5 Jpdi] DnaJ homolog subfamily C member 10 (EC 1.8.4.-) (Endoplasmic reticulum DNA J domain-containing protein 5) (ER-resident protein ERdj5) (ERdj5) (Endoplasmic reticulum DnaJ-PDI fusion protein 1) (J domain-containing protein disulfide isomerase-like protein) (J domain-containing PDI-like protein) (JPDI)
[DNAJB11] DnaJ homolog subfamily B member 11 (ER-associated DNAJ) (ER-associated Hsp40 co-chaperone) (Endoplasmic reticulum DNA J domain-containing protein 3) (ER-resident protein ERdj3) (ERdj3) (ERj3p)
[DNAJB11] DnaJ homolog subfamily B member 11 (ER-associated DNAJ) (ER-associated Hsp40 co-chaperone) (Endoplasmic reticulum DNA J domain-containing protein 3) (ER-resident protein ERdj3) (ERdj3) (ERj3p)
[DNAJB11] DnaJ homolog subfamily B member 11 (ER-associated DNAJ) (ER-associated Hsp40 co-chaperone) (Endoplasmic reticulum DNA J domain-containing protein 3) (ER-resident protein ERdj3) (ERdj3) (ERj3p)
[DNAJC10 ERDJ5 UNQ495/PRO1012] DnaJ homolog subfamily C member 10 (EC 1.8.4.-) (Endoplasmic reticulum DNA J domain-containing protein 5) (ER-resident protein ERdj5) (ERdj5) (Macrothioredoxin) (MTHr)
[DNAJA1 DNAJ2 HDJ2 HSJ2 HSPF4] DnaJ homolog subfamily A member 1 (DnaJ protein homolog 2) (HSDJ) (Heat shock 40 kDa protein 4) (Heat shock protein J2) (HSJ-2) (Human DnaJ protein 2) (hDj-2)
[Dnajb2 Dnajb10] DnaJ homolog subfamily B member 2 (DnaJ homolog subfamily B member 10) (mDj8)
[Dnaja1 Dnaj2 Hsj2 Hspf4] DnaJ homolog subfamily A member 1 (DnaJ protein homolog 2) (Heat shock 40 kDa protein 4) (Heat shock protein J2) (HSJ-2)
[DNAJB2 HSJ1 HSPF3] DnaJ homolog subfamily B member 2 (Heat shock 40 kDa protein 3) (Heat shock protein J1) (HSJ-1)
[DNAJB12] DnaJ homolog subfamily B member 12
[DNAJC2 MPHOSPH11 MPP11 ZRF1] 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]
[DNAJA3 HCA57 TID1] DnaJ homolog subfamily A member 3, mitochondrial (DnaJ protein Tid-1) (hTid-1) (Hepatocellular carcinoma-associated antigen 57) (Tumorous imaginal discs protein Tid56 homolog)
[Dnaja1 Hsj2 Rdj1] DnaJ homolog subfamily A member 1 (DnaJ-like protein 1) (Heat shock protein J2) (HSJ-2)
[DNAJB14 UNQ9427/PRO34683] DnaJ homolog subfamily B member 14
[Dnaja3 Tid1] DnaJ homolog subfamily A member 3, mitochondrial (DnaJ protein Tid-1) (mTid-1) (Tumorous imaginal discs protein Tid56 homolog)
[Hspa5 Grp78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[Pdia4 Cabp2 Erp70] Protein disulfide-isomerase A4 (EC 5.3.4.1) (Calcium-binding protein 2) (CaBP2) (Endoplasmic reticulum resident protein 70) (ER protein 70) (ERp70) (Endoplasmic reticulum resident protein 72) (ER protein 72) (ERp-72) (ERp72)
[TXNDC12 TLP19 UNQ713/PRO1376] Thioredoxin domain-containing protein 12 (EC 1.8.4.2) (Endoplasmic reticulum resident protein 18) (ER protein 18) (ERp18) (Endoplasmic reticulum resident protein 19) (ER protein 19) (ERp19) (Thioredoxin-like protein p19) (hTLP19)
[MAN1B1 UNQ747/PRO1477] Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase (EC 3.2.1.113) (ER alpha-1,2-mannosidase) (ER mannosidase 1) (ERMan1) (Man9GlcNAc2-specific-processing alpha-mannosidase) (Mannosidase alpha class 1B member 1)
[DNAJC5 CLN4] DnaJ homolog subfamily C member 5 (Ceroid-lipofuscinosis neuronal protein 4) (Cysteine string protein) (CSP)
[PDIA3 ERP57 ERP60 GRP58] Protein disulfide-isomerase A3 (EC 5.3.4.1) (58 kDa glucose-regulated protein) (58 kDa microsomal protein) (p58) (Disulfide isomerase ER-60) (Endoplasmic reticulum resident protein 57) (ER protein 57) (ERp57) (Endoplasmic reticulum resident protein 60) (ER protein 60) (ERp60)
[P4hb Pdia1] Protein disulfide-isomerase (PDI) (EC 5.3.4.1) (Cellular thyroid hormone-binding protein) (Endoplasmic reticulum resident protein 59) (ER protein 59) (ERp59) (Prolyl 4-hydroxylase subunit beta) (p55)
[dnaJ groP b0015 JW0014] Chaperone protein DnaJ (HSP40) (Heat shock protein J)
[DNAJA1] DnaJ homolog subfamily A member 1 (DnaJ protein homolog 2) (DJ-2) (Mydj2)
[ERP44 KIAA0573 TXNDC4 UNQ532/PRO1075] Endoplasmic reticulum resident protein 44 (ER protein 44) (ERp44) (Thioredoxin domain-containing protein 4)
[PDIA4 ERP70 ERP72] Protein disulfide-isomerase A4 (EC 5.3.4.1) (Endoplasmic reticulum resident protein 70) (ER protein 70) (ERp70) (Endoplasmic reticulum resident protein 72) (ER protein 72) (ERp-72) (ERp72)
[DNAJC24 DPH4 ZCSL3] DnaJ homolog subfamily C member 24 (CSL-type zinc finger-containing protein 3) (Diphthamide biosynthesis protein 4)

Bibliography :