P32589
Gene name |
SSE1 (MSI3, YPL106C, LPG3C) |
Protein name |
Heat shock protein homolog SSE1 |
Names |
Chaperone protein MSI3 |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YPL106C |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
5 structures for P32589
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 2QXL | X-ray | 241 A | A/B | 2-659 | PDB |
| 3C7N | X-ray | 312 A | A | 1-666 | PDB |
| 3D2E | X-ray | 235 A | PDB | ||
| 3D2F | X-ray | 230 A | PDB | ||
| AF-P32589-F1 | Predicted | AlphaFoldDB |
3 variants for P32589
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s16-351855 | 140 | D>N | No | SGRP | |
| s16-350651 | 541 | G>A | No | SGRP | |
| s16-350201 | 691 | D>G | No | SGRP |
No associated diseases with P32589
2 regional properties for P32589
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Heat shock protein 70, conserved site | 201 - 214 | IPR018181-1 |
| conserved_site | Heat shock protein 70, conserved site | 338 - 352 | IPR018181-2 |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
| polysome | A multiribosomal structure representing a linear array of ribosomes held together by messenger RNA. They represent the active complexes in cellular protein synthesis and are able to incorporate amino acids into polypeptides both in vivo and in vitro. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| adenyl-nucleotide exchange factor activity | Binds to and stimulates the hydrolysis and exchange of adenyl nucleotides by other proteins. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP-dependent protein folding chaperone | Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis. |
| calmodulin binding | Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states. |
| peptide binding | Binding to a peptide, an organic compound comprising two or more amino acids linked by peptide bonds. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| autophagy | The cellular catabolic process in which cells digest parts of their own cytoplasm; allows for both recycling of macromolecular constituents under conditions of cellular stress and remodeling the intracellular structure for cell differentiation. |
| proteasomal ubiquitin-independent protein catabolic process | The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds that is mediated by the proteasome but do not involve ubiquitin. |
| proteasome-mediated ubiquitin-dependent protein catabolic process | The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome. |
| protein folding | The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. |
| protein refolding | The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones. |
5 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P32590 | SSE2 | Heat shock protein homolog SSE2 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
| O95757 | HSPA4L | Heat shock 70 kDa protein 4L | Homo sapiens (Human) | PR |
| P48722 | Hspa4l | Heat shock 70 kDa protein 4L | Mus musculus (Mouse) | PR |
| Q61316 | Hspa4 | Heat shock 70 kDa protein 4 | Mus musculus (Mouse) | PR |
| Q05036 | hsp-110 | Heat shock protein 110 | Caenorhabditis elegans | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSTPFGLDLG | NNNSVLAVAR | NRGIDIVVNE | VSNRSTPSVV | GFGPKNRYLG | ETGKNKQTSN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| IKNTVANLKR | IIGLDYHHPD | FEQESKHFTS | KLVELDDKKT | GAEVRFAGEK | HVFSATQLAA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| MFIDKVKDTV | KQDTKANITD | VCIAVPPWYT | EEQRYNIADA | ARIAGLNPVR | IVNDVTAAGV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SYGIFKTDLP | EGEEKPRIVA | FVDIGHSSYT | CSIMAFKKGQ | LKVLGTACDK | HFGGRDFDLA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ITEHFADEFK | TKYKIDIREN | PKAYNRILTA | AEKLKKVLSA | NTNAPFSVES | VMNDVDVSSQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LSREELEELV | KPLLERVTEP | VTKALAQAKL | SAEEVDFVEI | IGGTTRIPTL | KQSISEAFGK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PLSTTLNQDE | AIAKGAAFIC | AIHSPTLRVR | PFKFEDIHPY | SVSYSWDKQV | EDEDHMEVFP |
| 430 | 440 | 450 | 460 | 470 | 480 |
| AGSSFPSTKL | ITLNRTGDFS | MAASYTDITQ | LPPNTPEQIA | NWEITGVQLP | EGQDSVPVKL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| KLRCDPSGLH | TIEEAYTIED | IEVEEPIPLP | EDAPEDAEQE | FKKVTKTVKK | DDLTIVAHTF |
| 550 | 560 | 570 | 580 | 590 | 600 |
| GLDAKKLNEL | IEKENEMLAQ | DKLVAETEDR | KNTLEEYIYT | LRGKLEEEYA | PFASDAEKTK |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LQGMLNKAEE | WLYDEGFDSI | KAKYIAKYEE | LASLGNIIRG | RYLAKEEEKK | QAIRSKQEAS |
| 670 | 680 | 690 | |||
| QMAAMAEKLA | AQRKAEAEKK | EEKKDTEGDV | DMD |