P17535 · JUND_HUMAN
- ProteinTranscription factor JunD
- GeneJUND
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids347 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Transcription factor binding AP-1 sites (PubMed:9989505).
Heterodimerizes with proteins of the FOS family to form an AP-1 transcription factor complex, thereby enhancing their DNA binding activity to an AP-1 consensus sequence 3'-TGA[GC]TCA-5' and enhancing their transcriptional activity (PubMed:28981703, PubMed:9989505).
Heterodimerizes with proteins of the FOS family to form an AP-1 transcription factor complex, thereby enhancing their DNA binding activity to an AP-1 consensus sequence 3'-TGA[GC]TCA-5' and enhancing their transcriptional activity (PubMed:28981703, PubMed:9989505).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTranscription factor JunD
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP17535
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_055247 | 20 | in dbSNP:rs41478151 | |||
Sequence: G → V | ||||||
Mutagenesis | 30 | Reduced interaction with MEN1. | ||||
Sequence: R → A | ||||||
Mutagenesis | 31 | Reduced interaction with MEN1. | ||||
Sequence: L → A | ||||||
Mutagenesis | 32 | Loss of interaction with MEN1. | ||||
Sequence: F → A | ||||||
Mutagenesis | 33 | Loss of interaction with MEN1. | ||||
Sequence: P → A | ||||||
Mutagenesis | 34 | Loss of interaction with MEN1. | ||||
Sequence: G → R | ||||||
Mutagenesis | 35 | Reduced interaction with MEN1. | ||||
Sequence: A → R | ||||||
Mutagenesis | 36 | Reduced interaction with MEN1. | ||||
Sequence: P → A | ||||||
Mutagenesis | 37 | Reduced interaction with MEN1. | ||||
Sequence: P → A | ||||||
Mutagenesis | 46 | Loss of phosphorylation; when associated with A-47. | ||||
Sequence: K → A | ||||||
Mutagenesis | 46 | Reduced interaction with MEN1; when associated with E-47. | ||||
Sequence: K → E | ||||||
Mutagenesis | 47 | Loss of phosphorylation; when associated with A-46. | ||||
Sequence: K → A | ||||||
Mutagenesis | 47 | Reduced interaction with MEN1; when associated with E-46. | ||||
Sequence: K → E | ||||||
Mutagenesis | 52 | Loss of phosphorylation; when associated with A-54. | ||||
Sequence: L → A | ||||||
Mutagenesis | 54 | Loss of phosphorylation; when associated with A-52. | ||||
Sequence: L → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 400 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue, disulfide bond.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000076442 | 1-347 | UniProt | Transcription factor JunD | |||
Sequence: METPFYGDEALSGLGGGASGSGGSFASPGRLFPGAPPTAAAGSMMKKDALTLSLSEQVAAALKPAAAPPPTPLRADGAPSAAPPDGLLASPDLGLLKLASPELERLIIQSNGLVTTTPTSSQFLYPKVAASEEQEFAEGFVKALEDLHKQNQLGAGAAAAAAAAAAGGPSGTATGSAPPGELAPAAAAPEAPVYANLSSYAGGAGGAGGAATVAFAAEPVPFPPPPPPGALGPPRLAALKDEPQTVPDVPSFGESPPLSPIDMDTQERIKAERKRLRNRIAASKCRKRKLERISRLEEKVKTLKSQNTELASTASLLREQVAQLKQKVLSHVNSGCQLLPQHQVPAY | |||||||
Modified residue (large scale data) | 27 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 43 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 71 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 90 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 90 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 100 | UniProt | Phosphoserine; by MAPK8 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 100 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 117 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 117 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 251 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 251 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 255 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 255 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 259 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 259 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Disulfide bond | 285 | UniProt | Interchain (with C-172 in FOSB) | ||||
Sequence: C |
Post-translational modification
Phosphorylated by MAP kinases MAPK8 and MAPK10; phosphorylation is inhibited in the presence of MEN1.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Heterodimer; binds DNA as a heterodimer (PubMed:28981703).
Component of an AP-1 transcription factor complex composed of JUN-FOS heterodimers (By similarity).
As part of the AP-1 transcription factor complex, forms heterodimers with FOS proteins, thereby binding to the AP-1 consensus sequence and stimulating transcription (By similarity).
Forms heterodimers with FOSB; thereby binding to the AP-1 consensus sequence (PubMed:28981703).
Interacts (via MBM motif) with MEN1; this interaction represses transcriptional activation (PubMed:22327296, PubMed:9989505).
Interacts with MAPK10; this interaction is inhibited in the presence of MEN1 (PubMed:22327296).
Component of an AP-1 transcription factor complex composed of JUN-FOS heterodimers (By similarity).
As part of the AP-1 transcription factor complex, forms heterodimers with FOS proteins, thereby binding to the AP-1 consensus sequence and stimulating transcription (By similarity).
Forms heterodimers with FOSB; thereby binding to the AP-1 consensus sequence (PubMed:28981703).
Interacts (via MBM motif) with MEN1; this interaction represses transcriptional activation (PubMed:22327296, PubMed:9989505).
Interacts with MAPK10; this interaction is inhibited in the presence of MEN1 (PubMed:22327296).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P17535 | ACTR3 P61158 | 2 | EBI-2682803, EBI-351428 | |
BINARY | P17535 | APP P05067 | 3 | EBI-2682803, EBI-77613 | |
BINARY | P17535 | ATF2 P15336 | 6 | EBI-2682803, EBI-1170906 | |
BINARY | P17535 | ATF3 P18847 | 3 | EBI-2682803, EBI-712767 | |
BINARY | P17535 | ATF7 P17544 | 2 | EBI-2682803, EBI-765623 | |
BINARY | P17535 | BATF Q16520 | 2 | EBI-2682803, EBI-749503 | |
BINARY | P17535 | BATF3 Q9NR55 | 5 | EBI-2682803, EBI-10312707 | |
BINARY | P17535 | FOS P01100 | 14 | EBI-2682803, EBI-852851 | |
BINARY | P17535 | FOSL2 P15408 | 6 | EBI-2682803, EBI-3893419 | |
XENO | P17535 | HBZ P0C746 | 2 | EBI-2682803, EBI-10890294 | |
BINARY | P17535 | MAPK10 P53779 | 2 | EBI-2682803, EBI-713543 | |
BINARY | P17535 | MDM2 Q00987 | 3 | EBI-2682803, EBI-389668 | |
XENO | P17535 | MDV005 Q9DGW5 | 2 | EBI-2682803, EBI-10889526 | |
BINARY | P17535 | MEN1 O00255-2 | 6 | EBI-2682803, EBI-9869387 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, motif, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-43 | Disordered | ||||
Sequence: METPFYGDEALSGLGGGASGSGGSFASPGRLFPGAPPTAAAGS | ||||||
Motif | 27-39 | Menin-binding motif (MBM) | ||||
Sequence: SPGRLFPGAPPTA | ||||||
Motif | 46-55 | MAP kinase docking motif; essential for its phosphorylation | ||||
Sequence: KKDALTLSLS | ||||||
Region | 62-86 | Disordered | ||||
Sequence: LKPAAAPPPTPLRADGAPSAAPPDG | ||||||
Region | 244-264 | Disordered | ||||
Sequence: QTVPDVPSFGESPPLSPIDMD | ||||||
Region | 268-295 | Basic motif | ||||
Sequence: RIKAERKRLRNRIAASKCRKRKLERISR | ||||||
Domain | 268-331 | bZIP | ||||
Sequence: RIKAERKRLRNRIAASKCRKRKLERISRLEEKVKTLKSQNTELASTASLLREQVAQLKQKVLSH | ||||||
Region | 296-324 | Leucine-zipper | ||||
Sequence: LEEKVKTLKSQNTELASTASLLREQVAQL |
Domain
Binds DNA via bZIP domain; DNA-binding is under control of cellular redox homeostasis (in vitro) (PubMed:28981703).
To enable DNA binding, the bZIP domain must undergo a conformational rearrangement which requires the reduction of the interchain disulfide bond between FosB and JunD (in vitro) (PubMed:28981703).
To enable DNA binding, the bZIP domain must undergo a conformational rearrangement which requires the reduction of the interchain disulfide bond between FosB and JunD (in vitro) (PubMed:28981703).
Sequence similarities
Belongs to the bZIP family. Jun subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length347
- Mass (Da)35,174
- Last updated2009-05-05 v3
- ChecksumFE85A1AA2B5B9597
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
U3KPR5 | U3KPR5_HUMAN | JUND | 166 |
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 24 | in Ref. 1; CAA40010 | ||||
Sequence: S → T | ||||||
Sequence conflict | 157 | in Ref. 1; CAA40010 | ||||
Sequence: A → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X56681 EMBL· GenBank· DDBJ | CAA40010.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
EF044249 EMBL· GenBank· DDBJ | ABJ53425.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK223630 EMBL· GenBank· DDBJ | BAD97350.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471106 EMBL· GenBank· DDBJ | EAW84684.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X51346 EMBL· GenBank· DDBJ | CAA35739.1 EMBL· GenBank· DDBJ | mRNA |