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Protein
Submitted name:

Heat shock 70kDa protein 8 isoform 2 variant

Gene
N/A
Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

Complete GO annotation...

Keywords - Biological processi

Stress responseImported

Keywords - Ligandi

ATP-bindingUniRule annotation, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Submitted name:
Heat shock 70kDa protein 8 isoform 2 variantImported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

PTM / Processingi

Proteomic databases

PaxDbiQ53HF2.
PRIDEiQ53HF2.

PTM databases

iPTMnetiQ53HF2.

Expressioni

Gene expression databases

GenevisibleiQ53HF2. HS.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
MAPK8IP2Q133872EBI-877761,EBI-722813
SH2D1BO147963EBI-877761,EBI-3923013

Protein-protein interaction databases

IntActiQ53HF2. 2 interactions.
STRINGi9606.ENSP00000227378.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3Q49X-ray1.54C486-493[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the heat shock protein 70 family.UniRule annotation

Phylogenomic databases

eggNOGiKOG0101. Eukaryota.
COG0443. LUCA.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
KOiK03283.

Family and domain databases

Gene3Di2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
PROSITEiPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Q53HF2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL
60 70 80 90 100
IGDAAKNQVA MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR
110 120 130 140 150
PKVQVEYKGE TKSFYPEEVS SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF
160 170 180 190 200
NDSQRQATKD AGTIAGLNVL RIINEPTAAA IAYGLDKKVG AERNVLIFDL
210 220 230 240 250
GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH FIAEFKRKHK
260 270 280 290 300
KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA
310 320 330 340 350
RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL
360 370 380 390 400
QDFFNGKELN KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS
410 420 430 440 450
LGIETAGGVT TVLIKRNTTI PIKQTQTFTT YSDNQPGVLI QVYEGERAMT
460 470 480 490
KDNNLLGKFE LTGMPGGMPG GFPGGGAPPS GGASSGPTIE EVD
Length:493
Mass (Da):53,500
Last modified:May 24, 2005 - v1
Checksum:i518CE1F703509AFA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11Imported

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK222628 mRNA. Translation: BAD96348.1.
RefSeqiNP_006588.1. NM_006597.5.
NP_694881.1. NM_153201.3.
UniGeneiHs.180414.

Genome annotation databases

GeneIDi3312.
KEGGihsa:3312.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK222628 mRNA. Translation: BAD96348.1.
RefSeqiNP_006588.1. NM_006597.5.
NP_694881.1. NM_153201.3.
UniGeneiHs.180414.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3Q49X-ray1.54C486-493[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ53HF2. 2 interactions.
STRINGi9606.ENSP00000227378.

PTM databases

iPTMnetiQ53HF2.

Proteomic databases

PaxDbiQ53HF2.
PRIDEiQ53HF2.

Protocols and materials databases

DNASUi3312.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3312.
KEGGihsa:3312.

Organism-specific databases

CTDi3312.

Phylogenomic databases

eggNOGiKOG0101. Eukaryota.
COG0443. LUCA.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
KOiK03283.

Miscellaneous databases

GenomeRNAii3312.
NextBioi13136.

Gene expression databases

GenevisibleiQ53HF2. HS.

Family and domain databases

Gene3Di2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
PROSITEiPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides."
    Maruyama K., Sugano S.
    Gene 138:171-174(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: CerebellumImported.
  2. "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library."
    Suzuki Y., Yoshitomo K., Maruyama K., Suyama A., Sugano S.
    Gene 200:149-156(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: CerebellumImported.
  3. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: CerebellumImported.
  4. "Molecular mechanism of the negative regulation of Smad1/5 protein by carboxyl terminus of Hsc70-interacting protein (CHIP)."
    Wang L., Liu Y.T., Hao R., Chen L., Chang Z., Wang H.R., Wang Z.X., Wu J.W.
    J. Biol. Chem. 286:15883-15894(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 486-493.

Entry informationi

Entry nameiQ53HF2_HUMAN
AccessioniPrimary (citable) accession number: Q53HF2
Entry historyi
Integrated into UniProtKB/TrEMBL: May 24, 2005
Last sequence update: May 24, 2005
Last modified: March 16, 2016
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.