| IED ID |
IndEnz0002008447 |
| Enzyme Type ID |
protease008447 |
| Protein Name |
Protein skinhead-1
|
| Gene Name |
skn-1 T19E7.2 |
| Organism |
Caenorhabditis elegans |
| Taxonomic Lineage |
cellular organisms
Eukaryota
Opisthokonta
Metazoa
Eumetazoa
Bilateria
Protostomia
Ecdysozoa
Nematoda (roundworms)
Chromadorea
Rhabditida
Rhabditina
Rhabditomorpha
Rhabditoidea
Rhabditidae
Peloderinae
Caenorhabditis
Caenorhabditis elegans
|
| Enzyme Sequence |
MGGSSRRQRSTSATRRDDKRRRRQCFSSVADDEEETTSIYGVSSIFIWILATSSLILVISSPSSNTSIQSSSYDRITTKHLLDNISPTFKMYTDSNNRNFDEVNHQHQQEQDFNGQSKYDYPQFNRPMGLRWRDDQRMMEYFMSNGPVETVPVMPILTEHPPASPFGRGPSTERPTTSSRYEYSSPSLEDIDLIDVLWRSDIAGEKGTRQVAPADQYECDLQTLTEKSTVAPLTAEENARYEDLSKGFYNGFFESFNNNQYQQKHQQQQREQIKTPTLEHPTQKAELEDDLFDEDLAQLFEDVSREEGQLNQLFDNKQQHPVINNVSLSEGIVYNQANLTEMQEMRDSCNQVSISTIPTTSTAQPETLFNVTDSQTVEQWLPTEVVPNDVFPTSNYAYIGMQNDSLQAVVSNGQIDYDHSYQSTGQTPLSPLIIGSSGRQQQTQTSPGSVTVTATATQSLFDPYHSQRHSFSDCTTDSSSTCSRLSSESPRYTSESSTGTHESRFYGKLAPSSGSRYQRSSSPRSSQSSIKIARVVPLASGQRKRGRQSKDEQLASDNELPVSAFQISEMSLSELQQVLKNESLSEYQRQLIRKIRRRGKNKVAARTCRQRRTDRHDKMSHYI |
| Enzyme Length |
623 |
| Uniprot Accession Number |
P34707 |
| Absorption |
|
| Active Site |
|
| Activity Regulation |
|
| Binding Site |
|
| Calcium Binding |
|
| catalytic Activity |
|
| DNA Binding |
|
| EC Number |
|
| Enzyme Function |
FUNCTION: Transcription factor required to specify the fate of ventral blastomeres in the early embryo, and postembryonically for the development of the intestine. Directly regulates expression of zygotically expressed med-1 and med-2 to direct mesendoderm development (PubMed:1547503, PubMed:11463373). Required for stl-1 mRNA up-regulation in response to oxidative stress and anoxia. Required for the up-regulation of gcs-1 and several glutathione-S-transferase mRNAs in response to oxidative stress generated during pathogenic bacterial infection (PubMed:22216003). Modulates oxidative stress responses in concert with transcriptional coregulator hcf-1 (PubMed:22568582). Regulates the transcription of genes associated with metabolism in response to changes in nutrient availability (PubMed:23040073). In neurons, involved in mitochondrial fusion and behavioral recovery during reoxygenation (PubMed:24385935). Required for riok-1 mRNA expression in the intestine (PubMed:25688864). Downstream of the let-60/Ras, mek-2 and pmk-1 pathway, positively regulates lifespan probably by preventing transcription of insulin-like peptides such as ins-39 (PubMed:20624915). Prevents degeneration of dopaminergic CEP neurons in response to high Al(3+) or Mn(2+) levels, probably by promoting the expression of glutathione-S-transferase gst-1 (PubMed:23106139, PubMed:23721876). {ECO:0000269|PubMed:11463373, ECO:0000269|PubMed:1547503, ECO:0000269|PubMed:20624915, ECO:0000269|PubMed:22216003, ECO:0000269|PubMed:22568582, ECO:0000269|PubMed:23040073, ECO:0000269|PubMed:23106139, ECO:0000269|PubMed:23721876, ECO:0000269|PubMed:24385935, ECO:0000269|PubMed:25688864}.; FUNCTION: [Isoform a]: Directed by the ER-associated degradation pathway (ERAD), mediates proteasomal homeostasis by regulating the expression of proteasomal subunits such as rpt-3 to confer resistance to proteasomal dysfunction. {ECO:0000269|PubMed:27528192}. |
| Temperature Dependency |
|
| PH Dependency |
|
| Pathway |
|
| nucleotide Binding |
|
| Features |
Alternative sequence (3); Chain (1); Compositional bias (4); Helix (4); Modified residue (2); Mutagenesis (5); Region (5); Turn (1) |
| Keywords |
3D-structure;Activator;Alternative splicing;Cytoplasm;DNA-binding;Developmental protein;Mitochondrion;Nucleus;Phosphoprotein;Reference proteome;Stress response;Transcription;Transcription regulation;Translation regulation |
| Interact With |
|
| Induction |
|
| Subcellular Location |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16166371, ECO:0000269|PubMed:22216003, ECO:0000269|PubMed:26920757, ECO:0000269|PubMed:7939715}. Cytoplasm {ECO:0000269|PubMed:16166371, ECO:0000269|PubMed:22216003, ECO:0000269|PubMed:26920757}. Note=In absence of stress, localizes in the cytoplasm of intestinal cells (PubMed:16166371, PubMed:22216003, PubMed:26920757). Upon paraquat or arsenite treatments or upon bacterial infection, localizes in the nucleus (PubMed:16166371, PubMed:22216003, PubMed:26920757). Nuclear localization is regulated by pmk-1-mediated phosphorylation (PubMed:16166371, PubMed:26920757). Nuclear localization is regulated by transcriptional coregulator hcf-1. {ECO:0000269|PubMed:16166371, ECO:0000269|PubMed:22216003, ECO:0000269|PubMed:22568582, ECO:0000269|PubMed:26920757}.; SUBCELLULAR LOCATION: [Isoform a]: Nucleus {ECO:0000269|PubMed:27528192}. Mitochondrion {ECO:0000269|PubMed:23040073}. Note=Localizes to the nucleus in response to proteasomal dysfunction. {ECO:0000269|PubMed:27528192}. |
| Modified Residue |
MOD_RES 164; /note="Phosphoserine; by pmk-1"; /evidence="ECO:0000269|PubMed:16166371, ECO:0000269|PubMed:26920757"; MOD_RES 430; /note="Phosphoserine; by pmk-1"; /evidence="ECO:0000269|PubMed:16166371, ECO:0000269|PubMed:26920757" |
| Post Translational Modification |
PTM: [Isoform a]: Cleaved by the aspartic protease ddi-1. {ECO:0000269|PubMed:27528192}. |
| Signal Peptide |
|
| Structure 3D |
X-ray crystallography (1) |
| Cross Reference PDB |
1SKN;
|
| Mapped Pubmed ID |
10778742;
11178279;
11684665;
12529635;
12781695;
12869585;
14551910;
14704431;
15489339;
15581881;
15737937;
15791247;
15935776;
15979606;
16084508;
16251270;
16777607;
16973439;
16979152;
17296929;
17417969;
17537795;
17538612;
17567664;
17897480;
17964427;
17989133;
18358814;
18927620;
18977344;
19064914;
19273594;
19428455;
19575768;
19605496;
19627265;
19783783;
19818340;
20090912;
20164922;
20351174;
20439776;
20523893;
20647387;
20700440;
20805557;
20855423;
21040400;
21177963;
21177967;
21367940;
21695230;
21765926;
21980473;
22240150;
22267497;
22286215;
22560223;
22560298;
22577361;
22656429;
22901814;
23064027;
23419779;
23516373;
23531831;
23540702;
23549480;
23555279;
23791784;
23800452;
23894595;
23957350;
23973804;
24068555;
24068940;
24194349;
24439388;
24453991;
24884423;
24889636;
24912676;
25242029;
25284427;
25399685;
25487147;
25517099;
25819561;
26056713;
26063786;
26196144;
26228940;
26232625;
26430702;
26621724;
26715089;
26721385;
26780296;
26828939;
26899496;
26913604;
26919641;
27370100;
27381188;
27420916;
27540856;
27557896;
27623524;
27776126;
27783623;
27783938;
27974198;
28272406;
28341649;
28428286;
28459841;
28600327;
28612944;
28766017;
28974696;
29346364;
29445761;
29793058;
30114261;
30166349;
30250464;
30682707;
30710163;
30973820;
31409866;
31816375;
32161088;
32502151;
32663368;
34197476;
34830338;
6593563;
7607073;
8348611;
8861906;
9303538;
9367437;
9872954;
|
| Motif |
|
| Gene Encoded By |
|
| Mass |
70,709 |
| Kinetics |
|
| Metal Binding |
|
| Rhea ID |
|
| Cross Reference Brenda |
|