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

Heat shock cognate 71 kDa protein (Heat shock 70 kDa protein 8)

 HSP7C_RAT               Reviewed;         646 AA.
P63018; P08109; P12225; Q4FZY7; Q62373; Q62374; Q62375;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
27-SEP-2017, entry version 135.
RecName: Full=Heat shock cognate 71 kDa protein;
AltName: Full=Heat shock 70 kDa protein 8;
Name=Hspa8; Synonyms=Hsc70, Hsc73;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3595567;
Sorger P.K., Pelham H.R.B.;
"Cloning and expression of a gene encoding hsc73, the major hsp70-like
protein in unstressed rat cells.";
EMBO J. 6:993-998(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3939319; DOI=10.1128/MCB.5.12.3476;
O'Malley K., Mauron A., Barchas J.D., Kedes L.;
"Constitutively expressed rat mRNA encoding a 70-kilodalton heat-
shock-like protein.";
Mol. Cell. Biol. 5:3476-3483(1985).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart, and Pituitary;
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).
[4]
PROTEIN SEQUENCE OF 4-36; 57-71; 77-108; 127-155; 160-171; 237-246;
300-319; 349-357; 424-447; 452-458; 518-526; 540-550; 584-597 AND
602-609, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U., Lubec S.;
Submitted (SEP-2007) to UniProtKB.
[5]
INTERACTION WITH DNAJC7.
PubMed=10567422; DOI=10.1074/jbc.274.48.34425;
Liu F.H., Wu S.J., Hu S.M., Hsiao C.D., Wang C.;
"Specific interaction of the 70-kDa heat shock cognate protein with
the tetratricopeptide repeats.";
J. Biol. Chem. 274:34425-34432(1999).
[6]
INTERACTION WITH SGTA.
PubMed=15708368; DOI=10.1016/j.abb.2004.12.020;
Liou S.T., Wang C.;
"Small glutamine-rich tetratricopeptide repeat-containing protein is
composed of three structural units with distinct functions.";
Arch. Biochem. Biophys. 435:253-263(2005).
[7]
STRUCTURE BY NMR OF 385-543.
PubMed=10373374; DOI=10.1006/jmbi.1999.2776;
Morshauser R.C., Hu W., Wang H., Pang Y., Flynn G.C.,
Zuiderweg E.R.P.;
"High-resolution solution structure of the 18 kDa substrate-binding
domain of the mammalian chaperone protein Hsc70.";
J. Mol. Biol. 289:1387-1403(1999).
-!- FUNCTION: Molecular chaperone implicated in a wide variety of
cellular processes, including protection of the proteome from
stress, folding and transport of newly synthesized polypeptides,
activation of proteolysis of misfolded proteins and the formation
and dissociation of protein complexes. Plays a pivotal role in the
protein quality control system, ensuring the correct folding of
proteins, the re-folding of misfolded proteins and controlling the
targeting of proteins for subsequent degradation. This is achieved
through cycles of ATP binding, ATP hydrolysis and ADP release,
mediated by co-chaperones. The co-chaperones have been shown to
not only regulate different steps of the ATPase cycle of HSP70,
but they also have an individual specificity such that one co-
chaperone may promote folding of a substrate while another may
promote degradation. The affinity of HSP70 for polypeptides is
regulated by its nucleotide bound state. In the ATP-bound form, it
has a low affinity for substrate proteins. However, upon
hydrolysis of the ATP to ADP, it undergoes a conformational change
that increases its affinity for substrate proteins. HSP70 goes
through repeated cycles of ATP hydrolysis and nucleotide exchange,
which permits cycles of substrate binding and release. The HSP70-
associated co-chaperones are of three types: J-domain co-
chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the
nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate
conversion of HSP70 from the ADP-bound to the ATP-bound state
thereby promoting substrate release), and the TPR domain
chaperones such as HOPX and STUB1. Acts as a repressor of
transcriptional activation. Inhibits the transcriptional
coactivator activity of CITED1 on Smad-mediated transcription.
Component of the PRP19-CDC5L complex that forms an integral part
of the spliceosome and is required for activating pre-mRNA
splicing. May have a scaffolding role in the spliceosome assembly
as it contacts all other components of the core complex. Binds
bacterial lipopolysaccharide (LPS) and mediates LPS-induced
inflammatory response, including TNF secretion. Participates in
the ER-associated degradation (ERAD) quality control pathway in
conjunction with J domain-containing co-chaperones and the E3
ligase STUB1. {ECO:0000250|UniProtKB:P11142}.
-!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
containing untranslated mRNAs. Interacts with PACRG. Interacts
with HSPH1/HSP105. Interacts with IRAK1BP1 and BAG1 (By
similarity). Interacts with DNAJC7 (PubMed:10567422). Interacts
with DNAJB12 (via J domain). Interacts with DNAJB14 (via J
domain). Interacts (via C-terminus) with the E3 ligase STUB1
forming a 210 kDa complex of one STUB1 and two HSPA8 molecules.
Interacts with CITED1 (via N-terminus); the interaction suppresses
the association of CITED1 to p300/CBP and Smad-mediated
transcription transactivation. Component of the PRP19-CDC5L
splicing complex composed of a core complex comprising a
homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three
less stably associated proteins CTNNBL1, CWC15 and HSPA8.
Interacts with TRIM5. Part of a complex composed at least of
ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A,
WDR5 and ZNF335; this complex may have a histone H3-specific
methyltransferase activity. Interacts with METTL21A. Following LPS
binding, may form a complex with CXCR4, GDF5 and HSP90AA1.
Interacts with PRKN. Interacts with FOXP3. Interacts with DNAJC9
(via J domain). Interacts with MLLT11. Interacts with RNF207.
Interacts with DNAJC21. Interacts with DNAJB2. Interacts with TTC1
(via TPR repeats) (By similarity). Interacts with SGTA (via TPR
repeats) (PubMed:15708368). Interacts with HSF1 (via
transactivation domain). Interacts with HOPX, STUB1, HSP40, HSP90,
BAG2 and BAG3 (By similarity). Interacts with DNAJC12 (By
similarity). {ECO:0000250|UniProtKB:P11142,
ECO:0000269|PubMed:10567422, ECO:0000269|PubMed:15708368}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Melanosome
{ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Cell membrane
{ECO:0000250}. Note=Localized in cytoplasmic mRNP granules
containing untranslated mRNAs. Translocates rapidly from the
cytoplasm to the nuclei, and especially to the nucleoli, upon heat
shock (By similarity). {ECO:0000250}.
-!- INDUCTION: Constitutively synthesized.
-!- DOMAIN: The N-terminal nucleotide binding domain (NBD) (also known
as the ATPase domain) is responsible for binding and hydrolyzing
ATP. The C-terminal substrate-binding domain (SBD) (also known as
peptide-binding domain) binds to the client/substrate proteins.
The two domains are allosterically coupled so that, when ATP is
bound to the NBD, the SBD binds relatively weakly to clients. When
ADP is bound in the NBD, a conformational change enhances the
affinity of the SBD for client proteins.
{ECO:0000250|UniProtKB:P11142}.
-!- PTM: Acetylated. {ECO:0000250|UniProtKB:P11142}.
-!- PTM: ISGylated. {ECO:0000250|UniProtKB:P11142}.
-!- PTM: Trimethylation at Lys-561 reduces fibrillar SNCA binding.
{ECO:0000250|UniProtKB:P11142}.
-!- SIMILARITY: Belongs to the heat shock protein 70 family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Y00054; CAA68265.1; -; Genomic_DNA.
EMBL; M11942; AAA41354.1; -; mRNA.
EMBL; BC061547; AAH61547.1; -; mRNA.
EMBL; BC098914; AAH98914.1; -; mRNA.
PIR; S07197; S07197.
RefSeq; NP_077327.1; NM_024351.2.
UniGene; Rn.120392; -.
UniGene; Rn.129299; -.
UniGene; Rn.201298; -.
PDB; 1CKR; NMR; -; A=385-543.
PDB; 1Q2G; Model; -; C=385-543.
PDB; 1UD0; X-ray; 3.45 A; A/B/C/D=542-646.
PDB; 2V7Z; X-ray; 3.50 A; A/B=1-543.
PDB; 7HSC; NMR; -; A=385-543.
PDBsum; 1CKR; -.
PDBsum; 1Q2G; -.
PDBsum; 1UD0; -.
PDBsum; 2V7Z; -.
PDBsum; 7HSC; -.
ProteinModelPortal; P63018; -.
SMR; P63018; -.
BioGrid; 246629; 16.
CORUM; P63018; -.
DIP; DIP-33262N; -.
IntAct; P63018; 9.
MINT; MINT-2514077; -.
STRING; 10116.ENSRNOP00000058593; -.
iPTMnet; P63018; -.
PhosphoSitePlus; P63018; -.
World-2DPAGE; 0004:P63018; -.
PaxDb; P63018; -.
PRIDE; P63018; -.
GeneID; 24468; -.
KEGG; rno:24468; -.
UCSC; RGD:621725; rat.
CTD; 3312; -.
RGD; 621725; Hspa8.
eggNOG; KOG0101; Eukaryota.
eggNOG; COG0443; LUCA.
HOVERGEN; HBG051845; -.
InParanoid; P63018; -.
KO; K03283; -.
PhylomeDB; P63018; -.
EvolutionaryTrace; P63018; -.
PRO; PR:P63018; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0032279; C:asymmetric synapse; IDA:RGD.
GO; GO:0005776; C:autophagosome; IDA:RGD.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0030425; C:dendrite; IDA:ParkinsonsUK-UCL.
GO; GO:0043198; C:dendritic shaft; IDA:RGD.
GO; GO:0043197; C:dendritic spine; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; IDA:RGD.
GO; GO:0005882; C:intermediate filament; IDA:RGD.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; ISS:UniProtKB.
GO; GO:1990836; C:lysosomal matrix; IDA:MGI.
GO; GO:0005765; C:lysosomal membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0005764; C:lysosome; IDA:RGD.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:1990124; C:messenger ribonucleoprotein complex; IDA:RGD.
GO; GO:0005874; C:microtubule; IDA:RGD.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0044309; C:neuron spine; IDA:ParkinsonsUK-UCL.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0043204; C:perikaryon; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0001917; C:photoreceptor inner segment; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0099524; C:postsynaptic cytosol; IDA:SynGO.
GO; GO:0014069; C:postsynaptic density of dendrite; IDA:ParkinsonsUK-UCL.
GO; GO:0099523; C:presynaptic cytosol; IDA:SynGO.
GO; GO:0043234; C:protein complex; IDA:RGD.
GO; GO:0000974; C:Prp19 complex; ISS:UniProtKB.
GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
GO; GO:0043195; C:terminal bouton; IDA:ParkinsonsUK-UCL.
GO; GO:0031686; F:A1 adenosine receptor binding; IPI:RGD.
GO; GO:0043531; F:ADP binding; IDA:RGD.
GO; GO:0005524; F:ATP binding; IDA:RGD.
GO; GO:0016887; F:ATPase activity; IDA:MGI.
GO; GO:0042623; F:ATPase activity, coupled; IDA:RGD.
GO; GO:1990833; F:clathrin-uncoating ATPase activity; IDA:RGD.
GO; GO:0019899; F:enzyme binding; IPI:RGD.
GO; GO:0042277; F:peptide binding; IDA:RGD.
GO; GO:1904593; F:prostaglandin binding; IPI:RGD.
GO; GO:0005102; F:receptor binding; IPI:RGD.
GO; GO:0003723; F:RNA binding; IDA:RGD.
GO; GO:0008134; F:transcription factor binding; IPI:RGD.
GO; GO:0051082; F:unfolded protein binding; IMP:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0008088; P:axo-dendritic transport; IEP:RGD.
GO; GO:0043624; P:cellular protein complex disassembly; IMP:MGI.
GO; GO:0071276; P:cellular response to cadmium ion; IEP:RGD.
GO; GO:0034605; P:cellular response to heat; IEP:RGD.
GO; GO:0021549; P:cerebellum development; IEP:RGD.
GO; GO:0051085; P:chaperone mediated protein folding requiring cofactor; IDA:RGD.
GO; GO:0061684; P:chaperone-mediated autophagy; IDA:ParkinsonsUK-UCL.
GO; GO:1904764; P:chaperone-mediated autophagy translocation complex disassembly; IDA:ParkinsonsUK-UCL.
GO; GO:0061077; P:chaperone-mediated protein folding; IDA:RGD.
GO; GO:0061741; P:chaperone-mediated protein transport involved in chaperone-mediated autophagy; IGI:MGI.
GO; GO:0072318; P:clathrin coat disassembly; IDA:RGD.
GO; GO:0044849; P:estrous cycle; IEP:RGD.
GO; GO:0030900; P:forebrain development; IEP:RGD.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEP:RGD.
GO; GO:0001822; P:kidney development; IEP:RGD.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IMP:RGD.
GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; IEP:RGD.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0043085; P:positive regulation of catalytic activity; IMP:RGD.
GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD.
GO; GO:0097214; P:positive regulation of lysosomal membrane permeability; IMP:RGD.
GO; GO:0050766; P:positive regulation of phagocytosis; IMP:RGD.
GO; GO:1904592; P:positive regulation of protein refolding; IDA:RGD.
GO; GO:0045862; P:positive regulation of proteolysis; IDA:RGD.
GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IMP:RGD.
GO; GO:0046777; P:protein autophosphorylation; IDA:RGD.
GO; GO:0006606; P:protein import into nucleus; IMP:RGD.
GO; GO:0042026; P:protein refolding; ISS:ParkinsonsUK-UCL.
GO; GO:0044743; P:protein transmembrane import into intracellular organelle; IEP:RGD.
GO; GO:0061635; P:regulation of protein complex stability; IDA:ParkinsonsUK-UCL.
GO; GO:0014823; P:response to activity; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0009408; P:response to heat; IEP:RGD.
GO; GO:0010045; P:response to nickel cation; IEP:RGD.
GO; GO:1990834; P:response to odorant; IEP:RGD.
GO; GO:0032570; P:response to progesterone; IEP:RGD.
GO; GO:0042594; P:response to starvation; IEP:RGD.
GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
GO; GO:0007608; P:sensory perception of smell; IEP:RGD.
GO; GO:0007519; P:skeletal muscle tissue development; IEP:RGD.
GO; GO:1990832; P:slow axonal transport; IEP:RGD.
GO; GO:0016191; P:synaptic vesicle uncoating; IC:SynGO.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.20.1270.10; -; 1.
Gene3D; 2.60.34.10; -; 1.
InterPro; IPR018181; Heat_shock_70_CS.
InterPro; IPR029048; HSP70_C.
InterPro; IPR029047; HSP70_peptide-bd.
InterPro; IPR013126; Hsp_70_fam.
Pfam; PF00012; HSP70; 1.
PRINTS; PR00301; HEATSHOCK70.
SUPFAM; SSF100920; SSF100920; 1.
SUPFAM; SSF100934; SSF100934; 1.
PROSITE; PS00297; HSP70_1; 1.
PROSITE; PS00329; HSP70_2; 1.
PROSITE; PS01036; HSP70_3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Cell membrane; Chaperone;
Complete proteome; Cytoplasm; Direct protein sequencing;
Isopeptide bond; Membrane; Methylation; mRNA processing;
mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Repressor; Spliceosome; Stress response;
Transcription; Transcription regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P11142}.
CHAIN 2 646 Heat shock cognate 71 kDa protein.
/FTId=PRO_0000078273.
NP_BIND 12 15 ATP. {ECO:0000250}.
NP_BIND 202 204 ATP. {ECO:0000250}.
NP_BIND 268 275 ATP. {ECO:0000250}.
NP_BIND 339 342 ATP. {ECO:0000250}.
REGION 2 386 Nucleotide-binding domain (NBD).
{ECO:0000250|UniProtKB:P11142}.
REGION 186 377 Interaction with BAG1. {ECO:0000250}.
REGION 394 509 Substrate-binding domain (SBD).
{ECO:0000250|UniProtKB:P11142}.
BINDING 71 71 ATP. {ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 108 108 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63017}.
MOD_RES 153 153 Phosphoserine.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 246 246 N6-acetyllysine.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 319 319 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 319 319 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63017}.
MOD_RES 328 328 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63017}.
MOD_RES 329 329 Phosphoserine.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 362 362 Phosphoserine.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 469 469 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 512 512 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P63017}.
MOD_RES 512 512 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63017}.
MOD_RES 524 524 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63017}.
MOD_RES 541 541 Phosphoserine.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 561 561 N6,N6,N6-trimethyllysine; by METTL21A;
alternate.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 561 561 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 589 589 N6-acetyllysine.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 597 597 N6-acetyllysine.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 601 601 N6-acetyllysine.
{ECO:0000250|UniProtKB:P11142}.
CROSSLNK 512 512 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P11142}.
CROSSLNK 512 512 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P11142}.
STRAND 6 10 {ECO:0000244|PDB:2V7Z}.
STRAND 13 22 {ECO:0000244|PDB:2V7Z}.
STRAND 25 28 {ECO:0000244|PDB:2V7Z}.
STRAND 32 34 {ECO:0000244|PDB:2V7Z}.
STRAND 41 44 {ECO:0000244|PDB:2V7Z}.
STRAND 49 52 {ECO:0000244|PDB:2V7Z}.
HELIX 53 58 {ECO:0000244|PDB:2V7Z}.
TURN 59 61 {ECO:0000244|PDB:2V7Z}.
STRAND 66 68 {ECO:0000244|PDB:2V7Z}.
TURN 71 75 {ECO:0000244|PDB:2V7Z}.
HELIX 81 86 {ECO:0000244|PDB:2V7Z}.
STRAND 91 97 {ECO:0000244|PDB:2V7Z}.
STRAND 100 105 {ECO:0000244|PDB:2V7Z}.
STRAND 112 114 {ECO:0000244|PDB:2V7Z}.
HELIX 116 135 {ECO:0000244|PDB:2V7Z}.
STRAND 141 146 {ECO:0000244|PDB:2V7Z}.
HELIX 152 165 {ECO:0000244|PDB:2V7Z}.
STRAND 168 174 {ECO:0000244|PDB:2V7Z}.
HELIX 175 182 {ECO:0000244|PDB:2V7Z}.
TURN 183 186 {ECO:0000244|PDB:2V7Z}.
STRAND 193 200 {ECO:0000244|PDB:2V7Z}.
STRAND 205 213 {ECO:0000244|PDB:2V7Z}.
STRAND 216 223 {ECO:0000244|PDB:2V7Z}.
HELIX 230 249 {ECO:0000244|PDB:2V7Z}.
HELIX 257 276 {ECO:0000244|PDB:2V7Z}.
STRAND 278 288 {ECO:0000244|PDB:2V7Z}.
STRAND 291 298 {ECO:0000244|PDB:2V7Z}.
HELIX 299 305 {ECO:0000244|PDB:2V7Z}.
HELIX 307 312 {ECO:0000244|PDB:2V7Z}.
HELIX 314 323 {ECO:0000244|PDB:2V7Z}.
HELIX 328 330 {ECO:0000244|PDB:2V7Z}.
STRAND 332 338 {ECO:0000244|PDB:2V7Z}.
HELIX 339 342 {ECO:0000244|PDB:2V7Z}.
HELIX 344 353 {ECO:0000244|PDB:2V7Z}.
TURN 354 356 {ECO:0000244|PDB:2V7Z}.
TURN 365 367 {ECO:0000244|PDB:2V7Z}.
HELIX 368 380 {ECO:0000244|PDB:2V7Z}.
STRAND 388 391 {ECO:0000244|PDB:1CKR}.
STRAND 396 399 {ECO:0000244|PDB:1CKR}.
STRAND 401 405 {ECO:0000244|PDB:1CKR}.
TURN 406 408 {ECO:0000244|PDB:1CKR}.
STRAND 409 411 {ECO:0000244|PDB:1CKR}.
STRAND 418 429 {ECO:0000244|PDB:1CKR}.
STRAND 431 434 {ECO:0000244|PDB:1CKR}.
STRAND 438 445 {ECO:0000244|PDB:1CKR}.
STRAND 447 450 {ECO:0000244|PDB:1CKR}.
STRAND 452 461 {ECO:0000244|PDB:1CKR}.
STRAND 468 470 {ECO:0000244|PDB:7HSC}.
STRAND 472 481 {ECO:0000244|PDB:1CKR}.
TURN 482 484 {ECO:0000244|PDB:1CKR}.
STRAND 485 492 {ECO:0000244|PDB:1CKR}.
TURN 493 496 {ECO:0000244|PDB:1CKR}.
STRAND 497 503 {ECO:0000244|PDB:1CKR}.
HELIX 511 518 {ECO:0000244|PDB:1CKR}.
TURN 519 521 {ECO:0000244|PDB:1CKR}.
HELIX 522 527 {ECO:0000244|PDB:1CKR}.
TURN 532 534 {ECO:0000244|PDB:1CKR}.
STRAND 537 541 {ECO:0000244|PDB:1CKR}.
HELIX 542 553 {ECO:0000244|PDB:1UD0}.
HELIX 556 558 {ECO:0000244|PDB:1UD0}.
TURN 559 561 {ECO:0000244|PDB:1UD0}.
HELIX 564 595 {ECO:0000244|PDB:1UD0}.
HELIX 597 610 {ECO:0000244|PDB:1UD0}.
SEQUENCE 646 AA; 70871 MW; 03A27B30E6C076ED CRC64;
MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA
MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR PKVQVEYKGE TKSFYPEEVS
SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF NDSQRQATKD AGTIAGLNVL RIINEPTAAA
IAYGLDKKVG AERNVLIFDL GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH
FIAEFKRKHK KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA
RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL QDFFNGKELN
KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS LGIETAGGVM TVLIKRNTTI
PTKQTQTFTT YSDNQPGVLI QVYEGERAMT KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI
DANGILNVSA VDKSTGKENK ITITNDKGRL SKEDIERMVQ EAEKYKAEDE KQRDKVSSKN
SLESYAFNMK ATVEDEKLQG KINDEDKQKI LDKCNEIISW LDKNQTAEKE EFEHQQKELE
KVCNPIITKL YQSAGGMPGG MPGGFPGGGA PPSGGASSGP TIEEVD


Related products :

Catalog number Product name Quantity
EIAAB11548 DnaJ homolog subfamily B member 5,DNAJB5,Heat shock protein cognate 40,Heat shock protein Hsp40-2,Heat shock protein Hsp40-3,Homo sapiens,Hsc40,HSC40,Human
MEDCLA337-1 Heat Shock Protein 70 (HSP70), Heat Shock Cognate Protein 70 (HSC70), Clone 8B11, Mab anti_Hu,Ms,Rt; prfn_NO frzn, IH_WB 1 ml.
MEDCLA337-01 Heat Shock Protein 70 (HSP70), Heat Shock Cognate Protein 70 (HSC70), Clone 8B11, Mab anti_Hu,Ms,Rt; prfn_NO frzn, IH_WB 0.1 ml.
AS05 083A rabbit polyclonal HSP70 per HSC70 Heat shock protein 70 per Heat shock cognate protein 70, Affinity purified 50
YSGSPP752B Heat Shock Cognate 70 (HSC70), Heat Shock Protein 73 (Hsp73), Bovine recombinant ATPase Fragment 20 µg.
YSGSPP752E Heat Shock Cognate 70 (HSC70), Heat Shock Protein 73 (Hsp73), Bovine recombinant ATPase Fragment 100 µg.
YSGSPP761B Heat Shock Cognate 70 (HSC70), Heat Shock Protein 73 (Hsp73), Bovine recombinant, Biotin conjugate 20 µg.
YSGSPP761E Heat Shock Cognate 70 (HSC70), Heat Shock Protein 73 (Hsp73), Bovine recombinant, Biotin conjugate 100 µg.
YSGSPA758E Heat Shock Protein 70 (Hsp70), Heat Shock Cognate 70 (Hsc70), ~72&73kD, Rabbit anti_Fish; WB 100 µl.
YSGSPA758C Heat Shock Protein 70 (Hsp70), Heat Shock Cognate 70 (Hsc70), ~72&73kD, Rabbit anti_Fish; WB 25 µl.
AS05 083 rabbit polyclonal HSP70 per HSC70 | Heat shock protein 70 per Heat shock cognate protein 70 (serum) 100
YSGSPP751E Heat Shock Cognate 70 (HSC70), Heat Shock Protein 73 (Hsp73), Bovine recombinant 100 µg.
YSGSPP751B Heat Shock Cognate 70 (HSC70), Heat Shock Protein 73 (Hsp73), Bovine recombinant 20 µg.
AS07 233 rabbit polyclonal HSC70 per HSP70 | heat shock cognate protein 70 per heat shock protein 70 100
EIAAB11549 DnaJ homolog subfamily B member 5,Dnajb5,Heat shock protein cognate 40,Heat shock protein Hsp40-3,Hsc40,Hsc40,Mouse,Mus musculus
YSGSPA822D Heat Shock Protein 70 (Hsp70), Heat Shock Cognate 70 (Hsc70), Inducible & Constitutive, ~72&73kD, Clone BB70, Mab anti_Chicken, Human, Mouse, Rat, Beluga, Bovine, Dog, Drosophila, Euglena gracilis, F 50 µg.
YSGSPA822F Heat Shock Protein 70 (Hsp70), Heat Shock Cognate 70 (Hsc70), Inducible & Constitutive, ~72&73kD, Clone BB70, Mab anti_Chicken, Human, Mouse, Rat, Beluga, Bovine, Dog, Drosophila, Euglena gracilis, F 200 µg.
10-663-45494 Heat Shock Protein 27kD (HSP27) Human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.05 mg
10-663-45494 Heat Shock Protein 27kD (HSP27) Human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.01 mg
10-663-45494 Heat Shock Protein 27kD (HSP27) Human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 1 mg
YSGSPA757E Heat Shock Protein 70 (Hsp70), Heat Shock Cognate 70 (Hsc70), Inducible & Constitutive, ~72&73kD, Rabbit anti_Rat, Human, Mouse, Bovine, Chicken, Dog, Drosophila, Fish, Guinea pig, Hamster, Monkey, Sw 100 µl.
YSGSPA820AP Heat Shock Protein 70 (Hsp70), Heat Shock Cognate 70 (Hsc70), Inducible & Constitutive, Rabbit anti_Human, Mouse, Rat, Beluga, Bovine, Dog, Chicken, Fish, Guinea pig, Hamster, Lobster, Monkey, Mussel, 200 µl.
YSGSPA820APD Heat Shock Protein 70 (Hsp70), Heat Shock Cognate 70 (Hsc70), Inducible & Constitutive, Rabbit anti_Human, Mouse, Rat, Beluga, Bovine, Dog, Chicken, Fish, Guinea pig, Hamster, Lobster, Monkey, Mussel, 50 µl.
YSGSPA820 Heat Shock Protein 70 (Hsp70), Heat Shock Cognate 70 (Hsc70), Inducible & Constitutive, Rabbit anti_Human, Mouse, Rat, Beluga, Bovine, Dog, Chicken, Fish, Guinea pig, Hamster, Lobster, Monkey, Mussel, 200 µg.
YSGSPA757C Heat Shock Protein 70 (Hsp70), Heat Shock Cognate 70 (Hsc70), Inducible & Constitutive, ~72&73kD, Rabbit anti_Rat, Human, Mouse, Bovine, Chicken, Dog, Drosophila, Fish, Guinea pig, Hamster, Monkey, Sw 25 µl.


 

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