| IED ID | IndEnz0005000409 |
| Enzyme Type ID | lipase000409 |
| Protein Name |
Cyclic AMP-responsive element-binding protein 3-like protein 3 cAMP-responsive element-binding protein 3-like protein 3 Transcription factor CREB-H Cleaved into: Processed cyclic AMP-responsive element-binding protein 3-like protein 3 |
| Gene Name | CREB3L3 CREBH HYST1481 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MNTDLAAGKMASAACSMDPIDSFELLDLLFDRQDGILRHVELGEGWGHVKDQQVLPNPDSDDFLSSILGSGDSLPSSPLWSPEGSDSGISEDLPSDPQDTPPRSGPATSPAGCHPAQPGKGPCLSYHPGNSCSTTTPGPVIQVPEASVTIDLEMWSPGGRICAEKPADPVDLSPRCNLTVKDLLLSGSSGDLQQHHLGASYLLRPGAGHCQELVLTEDEKKLLAKEGITLPTQLPLTKYEERVLKKIRRKIRNKQSAQESRKKKKEYIDGLETRMSACTAQNQELQRKVLHLEKQNLSLLEQLKKLQAIVVQSTSKSAQTGTCVAVLLLSFALIILPSISPFGPNKTESPGDFAPVRVFSRTLHNDAASRVAADAVPGSEAPGPRPEADTTREESPGSPGADWGFQDTANLTNSTEELDNATLVLRNATEGLGQVALLDWVAPGPSTGSGRAGLEAAGDEL |
| Enzyme Length | 461 |
| Uniprot Accession Number | Q68CJ9 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Transcription factor that may act during endoplasmic reticulum stress by activating unfolded protein response target genes. Activated in response to cAMP stimulation. In vitro, binds to the cAMP response element (CRE) and box-B element. Activates transcription through box-B element. Activates transcription through CRE (By similarity). May function synergistically with ATF6. In acute inflammatory response, may activate expression of acute phase response (APR) genes. May be involved in growth suppression. Regulates FGF21 transcription (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q91XE9, ECO:0000269|PubMed:11353085, ECO:0000269|PubMed:15800215, ECO:0000269|PubMed:16469704}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (4); Chain (2); Compositional bias (1); Cross-link (1); Domain (1); Frameshift (1); Glycosylation (5); Modified residue (1); Mutagenesis (2); Region (5); Sequence caution (1); Sequence conflict (1); Site (1); Topological domain (2); Transmembrane (1) |
| Keywords | Activator;Alternative splicing;DNA-binding;Endoplasmic reticulum;Glycoprotein;Isopeptide bond;Membrane;Nucleus;Phosphoprotein;Reference proteome;Signal-anchor;Transcription;Transcription regulation;Transmembrane;Transmembrane helix;Ubl conjugation;Unfolded protein response |
| Interact With | P18850; Q96LK0; O43889; Q96BA8; Itself; Q8NBI2; Q9C005; Q969F0; O00155; Q96EZ8; Q5J8X5; Q16649; Q02094; Q96GQ5; O43765; Q96EQ0; Q9NVC3; Q9NUM3; Q13190; Q8N8B7-2; Q8WW34-2; Q9Y228; Q96EC8 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11353085}; Single-pass type II membrane protein {ECO:0000269|PubMed:11353085}.; SUBCELLULAR LOCATION: [Processed cyclic AMP-responsive element-binding protein 3-like protein 3]: Nucleus {ECO:0000269|PubMed:30389664}. Note=Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus. |
| Modified Residue | MOD_RES 173; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:24275569 |
| Post Translational Modification | PTM: Controlled by regulated intramembrane proteolysis (RIP). Following ER stress a fragment containing the cytoplasmic transcription factor domain is released by proteolysis. The cleavage seems to be performed sequentially by site-1 and site-2 proteases (PS1 and PS2). {ECO:0000269|PubMed:16469704}.; PTM: N- and O-glycosylated. N-glycosylation is required for optimal proteolytic activation. O-glycosylated with core 1 or possibly core 8 glycans. {ECO:0000269|PubMed:20356926, ECO:0000269|PubMed:22171320}.; PTM: Ubiquitinated at Lys-294 by SYNV1/HRD1 via 'Lys-27'-linked ubiquitin. {ECO:0000269|PubMed:30389664}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12039695; 16236796; 16713569; 17875199; 18704925; 19361614; 19679815; 19883396; 20102225; 21666694; 21693703; 21719679; 21988832; 22262056; 23957007; 25428452; 26427795; 27029215; 28381424; 29738435; 32580631; 34491909; |
| Motif | |
| Gene Encoded By | |
| Mass | 49,077 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |