Q9NZI7 · UBIP1_HUMAN
- ProteinUpstream-binding protein 1
- GeneUBP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids540 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Functions as a transcriptional activator in a promoter context-dependent manner. Modulates the placental expression of CYP11A1. Involved in regulation of the alpha-globin gene in erythroid cells. Activation of the alpha-globin promoter in erythroid cells is via synergistic interaction with TFCP2 (By similarity).
Involved in regulation of the alpha-globin gene in erythroid cells. Binds strongly to sequences around the HIV-1 initiation site and weakly over the TATA-box. Represses HIV-1 transcription by inhibiting the binding of TFIID to the TATA-box
Involved in regulation of the alpha-globin gene in erythroid cells. Binds strongly to sequences around the HIV-1 initiation site and weakly over the TATA-box. Represses HIV-1 transcription by inhibiting the binding of TFIID to the TATA-box
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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Aspect | Term | |
---|---|---|
Cellular Component | chromatin | |
Cellular Component | cytosol | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | DNA-binding transcription activator activity, RNA polymerase II-specific | |
Molecular Function | DNA-binding transcription factor activity, RNA polymerase II-specific | |
Molecular Function | RNA polymerase II cis-regulatory region sequence-specific DNA binding | |
Molecular Function | sequence-specific double-stranded DNA binding | |
Biological Process | angiogenesis | |
Biological Process | negative regulation of viral transcription | |
Biological Process | positive regulation of transcription by RNA polymerase II | |
Biological Process | regulation of transcription by RNA polymerase II |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameUpstream-binding protein 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9NZI7
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_049294 | 109 | in dbSNP:rs3736563 | |||
Sequence: N → S | ||||||
Natural variant | VAR_025730 | 212 | in dbSNP:rs17854430 | |||
Sequence: T → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 460 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000229026 | 1-540 | UniProt | Upstream-binding protein 1 | |||
Sequence: MAWVLKMDEVIESGLVHDFDASLSGIGQELGAGAYSMSDVLALPIFKQEDSSLPLDGETEHPPFQYVMCAATSPAVKLHDETLTYLNQGQSYEIRMLDNRKMGDMPEINGKLVKSIIRVVFHDRRLQYTEHQQLEGWKWNRPGDRLLDLDIPMSVGIIDTRTNPSQLNAVEFLWDPAKRTSAFIQVHCISTEFTPRKHGGEKGVPFRIQVDTFKQNENGEYTDHLHSASCQIKVFKPKGADRKQKTDREKMEKRTAHEKEKYQPSYDTTILTEMRLEPIIEDAVEHEQKKSSKRTLPADYGDSLAKRGSCSPWPDAPTAYVNNSPSPAPTFTSPQQSTCSVPDSNSSSPNHQGDGASQTSGEQIQPSATIQETQQWLLKNRFSSYTRLFSNFSGADLLKLTKEDLVQICGAADGIRLYNSLKSRSVRPRLTIYVCREQPSSTVLQGQQQAASSASENGSGAPYVYHAIYLEEMIASEVARKLALVFNIPLHQINQVYRQGPTGIHILVSDQMVQNFQDESCFLFSTVKAESSDGIHIILK | |||||||
Modified residue | 22 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 194 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 390 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 390 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 393 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 393 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in adrenal tissue, JEG-3, NCI-H295A, Hep-G2 and HeLa cell lines.
Induction
By HIV-1 infection of lymphocytes.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with TFCP2. Interacts with PIAS1, and is probably part of a complex containing TFCP2, UBP1 and PIAS1 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9NZI7 | LNX1 Q8TBB1 | 3 | EBI-2795133, EBI-739832 | |
BINARY | Q9NZI7 | MORF4L1 Q9UBU8-2 | 3 | EBI-2795133, EBI-10288852 | |
BINARY | Q9NZI7 | TFCP2 Q12800 | 3 | EBI-2795133, EBI-717422 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 60-296 | Grh/CP2 DB | ||||
Sequence: EHPPFQYVMCAATSPAVKLHDETLTYLNQGQSYEIRMLDNRKMGDMPEINGKLVKSIIRVVFHDRRLQYTEHQQLEGWKWNRPGDRLLDLDIPMSVGIIDTRTNPSQLNAVEFLWDPAKRTSAFIQVHCISTEFTPRKHGGEKGVPFRIQVDTFKQNENGEYTDHLHSASCQIKVFKPKGADRKQKTDREKMEKRTAHEKEKYQPSYDTTILTEMRLEPIIEDAVEHEQKKSSKRTL | ||||||
Compositional bias | 236-264 | Basic and acidic residues | ||||
Sequence: KPKGADRKQKTDREKMEKRTAHEKEKYQP | ||||||
Region | 236-270 | Disordered | ||||
Sequence: KPKGADRKQKTDREKMEKRTAHEKEKYQPSYDTTI | ||||||
Region | 285-368 | Disordered | ||||
Sequence: EHEQKKSSKRTLPADYGDSLAKRGSCSPWPDAPTAYVNNSPSPAPTFTSPQQSTCSVPDSNSSSPNHQGDGASQTSGEQIQPSA | ||||||
Compositional bias | 316-368 | Polar residues | ||||
Sequence: APTAYVNNSPSPAPTFTSPQQSTCSVPDSNSSSPNHQGDGASQTSGEQIQPSA |
Sequence similarities
Belongs to the grh/CP2 family. CP2 subfamily.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9NZI7-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsLBP-1b
- Length540
- Mass (Da)60,491
- Last updated2000-10-01 v1
- ChecksumCD95819AA86A7F39
Q9NZI7-4
- Name2
- SynonymsLBP-1a
- Differences from canonical
- 274-309: Missing
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 93-94 | in Ref. 3; BAB14501 | ||||
Sequence: EI → D | ||||||
Compositional bias | 236-264 | Basic and acidic residues | ||||
Sequence: KPKGADRKQKTDREKMEKRTAHEKEKYQP | ||||||
Sequence conflict | 273 | in Ref. 1 | ||||
Sequence: E → EE | ||||||
Alternative sequence | VSP_017730 | 274-309 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 291-297 | in Ref. 1 | ||||
Sequence: SSKRTLP → VQQADFA | ||||||
Compositional bias | 316-368 | Polar residues | ||||
Sequence: APTAYVNNSPSPAPTFTSPQQSTCSVPDSNSSSPNHQGDGASQTSGEQIQPSA | ||||||
Sequence conflict | 418 | in Ref. 1 | ||||
Sequence: Y → V | ||||||
Sequence conflict | 424 | in Ref. 5; CAH18658 | ||||
Sequence: R → RR | ||||||
Sequence conflict | 503 | in Ref. 1 | ||||
Sequence: G → GH |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF198487 EMBL· GenBank· DDBJ | AAF32274.1 EMBL· GenBank· DDBJ | mRNA | ||
AK023274 EMBL· GenBank· DDBJ | BAB14501.1 EMBL· GenBank· DDBJ | mRNA | ||
BC047235 EMBL· GenBank· DDBJ | AAH47235.1 EMBL· GenBank· DDBJ | mRNA | ||
CR749798 EMBL· GenBank· DDBJ | CAH18658.1 EMBL· GenBank· DDBJ | mRNA |