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1.A.33.1.3
Heat shock protein 70(1B)

Accession Number:P08107
Protein Name:HSP70(1B)
Length:641
Molecular Weight:70052.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Cytoplasm1
Substrate ions

Cross database links:

Genevestigator: P08107
eggNOG: maNOG16200
HEGENOM: HBG334976
DIP: DIP-211N
RefSeq: NP_005336.3    NP_005337.2   
Entrez Gene ID: 3303    3304   
Pfam: PF00012   
Drugbank: Drugbank Link   
OMIM: 140550  gene
603012  gene
KEGG: hsa:3303    hsa:3304   

Gene Ontology

GO:0005783 C:endoplasmic reticulum
GO:0016234 C:inclusion body
GO:0005739 C:mitochondrion
GO:0016607 C:nuclear speck
GO:0048471 C:perinuclear region of cytoplasm
GO:0030529 C:ribonucleoprotein complex
GO:0005524 F:ATP binding
GO:0044183 F:protein binding involved in protein folding
GO:0047485 F:protein N-terminus binding
GO:0031625 F:ubiquitin protein ligase binding
GO:0051082 F:unfolded protein binding
GO:0006916 P:anti-apoptosis
GO:0006402 P:mRNA catabolic process
GO:0030308 P:negative regulation of cell growth
GO:0008285 P:negative regulation of cell proliferation
GO:0090084 P:negative regulation of inclusion body assembly
GO:0042026 P:protein refolding
GO:0006986 P:response to unfolded protein

References (22)

[1] “Structure and expression of the three MHC-linked HSP70 genes.”  Milner C.M.et.al.   1700760
[2] “Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70.”  Hunt C.et.al.   3931075
[3] “Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse.”  Xie T.et.al.   14656967
[4] “The DNA sequence and analysis of human chromosome 6.”  Mungall A.J.et.al.   14574404
[5] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[6] “Human major histocompatibility complex contains genes for the major heat shock protein HSP70.”  Sargent C.A.et.al.   2538825
[7] “In vitro transcription of a human hsp 70 heat shock gene by extracts prepared from heat-shocked and non-heat-shocked human cells.”  Drabent B.et.al.   3786141
[8] “Stable association of hsp90 and p23, but Not hsp70, with active human telomerase.”  Forsythe H.L.et.al.   11274138
[9] “Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system.”  Brychzy A.et.al.   12853476
[10] “Phosphorylation and binding partner analysis of the TSC1-TSC2 complex.”  Nellist M.et.al.   15963462
[11] “Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.”  Olsen J.V.et.al.   17081983
[12] “The disordered amino-terminus of SIMPL interacts with members of the 70-kDa heat-shock protein family.”  Haag Breese E.et.al.   17233114
[13] “The peptide-binding and ATPase domains of recombinant hsc70 are required to interact with rotavirus and reduce its infectivity.”  Perez-Vargas J.et.al.   16537599
[14] “A probability-based approach for high-throughput protein phosphorylation analysis and site localization.”  Beausoleil S.A.et.al.   16964243
[15] “Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.”  Rikova K.et.al.   18083107
[16] “Molecular composition of IMP1 ribonucleoprotein granules.”  Joeson L.et.al.   17289661
[17] “Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.”  Molina H.et.al.   17287340
[18] “Role of the cochaperone Tpr2 in Hsp90 chaperoning.”  Moffatt N.S.et.al.   18620420
[19] “Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.”  Daub H.et.al.   18691976
[20] “Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.”  Gauci S.et.al.   19413330
[21] “Lysine acetylation targets protein complexes and co-regulates major cellular functions.”  Choudhary C.et.al.   19608861
[22] “Structure of a new crystal form of human hsp70 ATPase domain.”  Osipiuk J.et.al.   10216320
Structure:
1HJO   1S3X   1XQS   2E88   2E8A   3D2E   3D2F   3JXU   3LOF      [...more]

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MAKAAAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA 
61:	LNPQNTVFDA KRLIGRKFGD PVVQSDMKHW PFQVINDGDK PKVQVSYKGE TKAFYPEEIS 
121:	SMVLTKMKEI AEAYLGYPVT NAVITVPAYF NDSQRQATKD AGVIAGLNVL RIINEPTAAA 
181:	IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVNH 
241:	FVEEFKRKHK KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA 
301:	RFEELCSDLF RSTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN 
361:	KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS LGLETAGGVM TALIKRNSTI 
421:	PTKQTQIFTT YSDNQPGVLI QVYEGERAMT KDNNLLGRFE LSGIPPAPRG VPQIEVTFDI 
481:	DANGILNVTA TDKSTGKANK ITITNDKGRL SKEEIERMVQ EAEKYKAEDE VQRERVSAKN 
541:	ALESYAFNMK SAVEDEGLKG KISEADKKKV LDKCQEVISW LDANTLAEKD EFEHKRKELE 
601:	QVCNPIISGL YQGAGGPGPG GFGAQGPKGG SGSGPTIEEV D