Description | Probable mediator of RNA polymerase II transcription subunit 37c |
Sequence | MAGKGEGPAIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPTNTVFDAKRLIGRRYSDPSVQADKSHWPFKVVSGPGEKPMIVVNHKGEEKQFSAEEISSMVLIKMREIAEAFLGSPVKNAVVTVPAYFNDSQRQATKDAGVISGLNVMRIINEPTAAAIAYGLDKKASSVGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNHFVQEFKRKNKKDITGNPRALRRLRTACERAKRTLSSTAQTTIEIDSLFEGIDFYTTITRARFEELNMDLFRKCMEPVEKCLRDAKMDKSSVHDVVLVGGSTRIPKVQQLLQDFFNGKELCKSINPDEAVAYGAAVQAAILSGEGNEKVQDLLLLDVTPLSLGLETAGGVMTVLIPRNTTIPTKKEQIFSTYSDNQPGVLIQVYEGERARTKDNNLLGKFELSGIPPAPRGVPQITVCFDIDANGILNVSAEDKTTGQKNKITITNDKGRLSKEEIEKMVQEAEKYKAEDEEHKKKVDAKNALENYAYNMRNTIKDEKIASKLDAADKKKIEDAIDQAIEWLDGNQLAEADEFEDKMKELESLCNPIIARMYQGAGPDMGGAGGMDDDTPAGGSGGAGPKIEEVD |
Length | 650 |
Position | Unknown |
Organism | Arabidopsis thaliana (Mouse-ear cress) |
Kingdom | Viridiplantae |
Lineage | Eukaryota> Viridiplantae> Streptophyta> Embryophyta> Tracheophyta> Spermatophyta> Magnoliopsida> eudicotyledons> Gunneridae> Pentapetalae> rosids> malvids> Brassicales> Brassicaceae> Camelineae> Arabidopsis. |
Aromaticity | 0.06 |
Grand average of hydropathy | -0.434 |
Instability index | 32.76 |
Isoelectric point | 5.14 |
Molecular weight | 71100.63 |
Publications | PubMed=10907853 PubMed=11130713 PubMed=27862469 PubMed=14593172 PubMed=11599561 PubMed=11402207 PubMed=11807141 PubMed=15805473 PubMed=17272265 PubMed=18065690 PubMed=19704521 PubMed=20028838 PubMed=22021418 PubMed=28004282 |
Annotated function |
In cooperation with other chaperones, Hsp70s are key
components that facilitate folding of de novo synthesized proteins,
assist translocation of precursor proteins into organelles, and are
responsible for degradation of damaged protein under stress conditions
(Probable). ATP-dependent molecular chaperone that assists folding of
unfolded or misfolded proteins under stress conditions. Mediates
plastid precursor degradation to prevent cytosolic precursor
accumulation, together with the E3 ubiquitin-protein ligase CHIP.
Recognizes specific sequence motifs in transit peptides and thereby led
to precursor degradation through the ubiquitin-proteasome system. Plays
a critical role in embryogenesis.
In cooperation with other chaperones, Hsp70s are key
components that facilitate folding of de novo synthesized proteins,
assist translocation of precursor proteins into organelles, and are
responsible for degradation of damaged protein under stress conditions.
ECO:0000269 PubMed:20028838 ECO:0000305 PubMed:11402207 ECO:0000305 |
GO - Cellular Component | cell wall GO:0005618 IDA:TAIR cytoplasm GO:0005737 IBA:GO_Central cytosol GO:0005829 IDA:TAIR Golgi apparatus GO:0005794 IDA:TAIR mitochondrion GO:0005739 IDA:TAIR nucleus GO:0005634 IEA:UniProtKB-SubCell plasma membrane GO:0005886 IDA:TAIR vacuolar membrane GO:0005774 IDA:TAIR |
GO - Biological Function | ATP binding GO:0005524 IDA:TAIR ATPase activity GO:0016887 IBA:GO_Central heat shock protein binding GO:0031072 IBA:GO_Central misfolded protein binding GO:0051787 IBA:GO_Central protein folding chaperone GO:0044183 IBA:GO_Central ubiquitin protein ligase binding GO:0031625 IPI:UniProtKB unfolded protein binding GO:0051082 IBA:GO_Central |
GO - Biological Process | cellular response to unfolded protein GO:0034620 IBA:GO_Central chaperone cofactor-dependent protein refolding GO:0051085 IBA:GO_Central protein refolding GO:0042026 IBA:GO_Central protein ubiquitination GO:0016567 IMUniProtKB response to bacterium GO:0009617 IETAIR response to cadmium ion GO:0046686 IETAIR response to heat GO:0009408 IEUniProtKB response to temperature stimulus GO:0009266 IETAIR response to virus GO:0009615 IETAIR |
Binary Interactions |
Repeats | >MDP31320 --------------------------------------------------------------------------- No. of Repeats|Total Score|Length |Diagonal| BW-From| BW-To| Level 2| 80.61| 25| 41| 511| 535| 1 --------------------------------------------------------------------------- 511- 535 (40.65/28.12) NDKGRLSKEEIEKMVQEAEKYKAED 554- 578 (39.96/27.52) NMRNTIKDEKIASKLDAADKKKIED --------------------------------------------------------------------------- --------------------------------------------------------------------------- No. of Repeats|Total Score|Length |Diagonal| BW-From| BW-To| Level 2| 134.03| 45| 189| 170| 218| 2 --------------------------------------------------------------------------- 170- 218 (62.42/54.19) GLNVMRIINePTaAAIAYGLDKKASSV.GEKNVLIFDLggGTFDVSLLTI 362- 407 (71.61/45.39) GKELCKSIN.PD.EAVAYGAAVQAAILsGEGNEKVQDL..LLLDVTPLSL --------------------------------------------------------------------------- --------------------------------------------------------------------------- No. of Repeats|Total Score|Length |Diagonal| BW-From| BW-To| Level 3| 76.19| 18| 21| 38| 55| 3 --------------------------------------------------------------------------- 16- 33 (19.09/ 9.17) ....TTYSCVGVWQHDRveIIA 38- 55 (32.57/20.02) NR..TTPSYVAFTDSER..LIG 60- 78 (24.54/13.56) NQvaMNPTNTVF.DAKR..LIG --------------------------------------------------------------------------- |
MoRF Sequence | Start | Stop |
1) GAGPKIEEVD 2) IARMY | 641 613 | 650 617 |
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Designed by Dr. Shailesh Lab & Dr. Jitendra K. Thakur Lab