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|---|---|
| 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 | ion |
Cross database links:
| DIP: | DIP-211N |
|---|---|
| RefSeq: | NP_005336.3 NP_005337.2 |
| Entrez Gene ID: | 3303 3304 |
| Pfam: | PF00012 |
| 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 | |
| Structure: | |
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| Predict TMSs (Predict number of transmembrane segments) | ||||
| FASTA formatted sequence |
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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