Q8NCF5 · NF2IP_HUMAN
- ProteinNFATC2-interacting protein
- GeneNFATC2IP
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids419 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
In T-helper 2 (Th2) cells, regulates the magnitude of NFAT-driven transcription of a specific subset of cytokine genes, including IL3, IL4, IL5 and IL13, but not IL2. Recruits PRMT1 to the IL4 promoter; this leads to enhancement of histone H4 'Arg-3'-methylation and facilitates subsequent histone acetylation at the IL4 locus, thus promotes robust cytokine expression (By similarity).
Down-regulates formation of poly-SUMO chains by UBE2I/UBC9 (By similarity).
Down-regulates formation of poly-SUMO chains by UBE2I/UBC9 (By similarity).
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 | cytoplasm | |
Cellular Component | nucleus | |
Biological Process | positive regulation of transcription by RNA polymerase II | |
Biological Process | protein sumoylation |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNFATC2-interacting protein
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8NCF5
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_031208 | 33 | in dbSNP:rs7201257 | |||
Sequence: R → W |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 490 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), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000281008 | 1-419 | UniProt | NFATC2-interacting protein | |||
Sequence: MAEPVGKRGRWSGGSGAGRGGRGGWGGRGRRPRAQRSPSRGTLDVVSVDLVTDSDEEILEVATARGAADEVEVEPPEPPGPVASRDNSNSDSEGEDRRPAGPPREPVRRRRRLVLDPGEAPLVPVYSGKVKSSLRLIPDDLSLLKLYPPGDEEEAELADSSGLYHEGSPSPGSPWKTKLRTKDKEEKKKTEFLDLDNSPLSPPSPRTKSRTHTRALKKLSEVNKRLQDLRSCLSPKPPQGQEQQGQEDEVVLVEGPTLPETPRLFPLKIRCRADLVRLPLRMSEPLQSVVDHMATHLGVSPSRILLLFGETELSPTATPRTLKLGVADIIDCVVLTSSPEATETSQQLQLRVQGKEKHQTLEVSLSRDSPLKTLMSHYEEAMGLSGRKLSFFFDGTKLSGRELPADLGMESGDLIEVWG | |||||||
Modified residue | 54 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 84 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 84 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 88 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 88 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 90 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 90 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 92 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 92 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 127 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 127 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 129 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 131 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 142 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 164 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 168 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 170 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 173 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 190 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 198 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 198 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 201 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 201 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 204 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 204 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 220 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 231 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 234 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 300 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 314 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 314 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 316 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 318 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 338 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 364 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 366 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 369 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 369 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 390 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 390 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Methylation at the N-terminus by PRMT1 modulates interaction with the NFAT complex and results in augmented cytokine production.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with NFATC2, TRAF1, TRAF2 and PRMT1. Interacts with UBE2I/UBC9 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8NCF5-2 | C22orf39 Q6P5X5 | 5 | EBI-12305293, EBI-7317823 | |
BINARY | Q8NCF5-2 | CALR P27797 | 3 | EBI-12305293, EBI-1049597 | |
BINARY | Q8NCF5-2 | CCDC157 Q569K6 | 3 | EBI-12305293, EBI-13289565 | |
BINARY | Q8NCF5-2 | DLST P36957 | 3 | EBI-12305293, EBI-351007 | |
BINARY | Q8NCF5-2 | DNAL4 O96015 | 6 | EBI-12305293, EBI-742362 | |
BINARY | Q8NCF5-2 | NEK7 Q8TDX7 | 3 | EBI-12305293, EBI-1055945 | |
BINARY | Q8NCF5-2 | NMNAT1 Q9HAN9 | 3 | EBI-12305293, EBI-3917542 | |
BINARY | Q8NCF5-2 | SNRPG P62308 | 3 | EBI-12305293, EBI-624585 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, coiled coil, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-131 | Disordered | ||||
Sequence: MAEPVGKRGRWSGGSGAGRGGRGGWGGRGRRPRAQRSPSRGTLDVVSVDLVTDSDEEILEVATARGAADEVEVEPPEPPGPVASRDNSNSDSEGEDRRPAGPPREPVRRRRRLVLDPGEAPLVPVYSGKVK | ||||||
Compositional bias | 89-116 | Basic and acidic residues | ||||
Sequence: NSDSEGEDRRPAGPPREPVRRRRRLVLD | ||||||
Region | 151-215 | Disordered | ||||
Sequence: DEEEAELADSSGLYHEGSPSPGSPWKTKLRTKDKEEKKKTEFLDLDNSPLSPPSPRTKSRTHTRA | ||||||
Compositional bias | 177-194 | Basic and acidic residues | ||||
Sequence: TKLRTKDKEEKKKTEFLD | ||||||
Coiled coil | 209-231 | |||||
Sequence: SRTHTRALKKLSEVNKRLQDLRS | ||||||
Domain | 348-419 | Ubiquitin-like | ||||
Sequence: LQLRVQGKEKHQTLEVSLSRDSPLKTLMSHYEEAMGLSGRKLSFFFDGTKLSGRELPADLGMESGDLIEVWG |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q8NCF5-1
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
- Length419
- Mass (Da)45,817
- Last updated2002-10-01 v1
- ChecksumCA04220B4BF0B245
Q8NCF5-2
- Name2
- Differences from canonical
- 1-281: Missing
Q8NCF5-3
- Name3
- Differences from canonical
- 1-292: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H3BSZ7 | H3BSZ7_HUMAN | NFATC2IP | 140 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_023932 | 1-281 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_023931 | 1-292 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 89-116 | Basic and acidic residues | ||||
Sequence: NSDSEGEDRRPAGPPREPVRRRRRLVLD | ||||||
Compositional bias | 177-194 | Basic and acidic residues | ||||
Sequence: TKLRTKDKEEKKKTEFLD |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK027545 EMBL· GenBank· DDBJ | BAB55189.1 EMBL· GenBank· DDBJ | mRNA | ||
AK074761 EMBL· GenBank· DDBJ | BAC11189.1 EMBL· GenBank· DDBJ | mRNA | ||
AK297333 EMBL· GenBank· DDBJ | BAH12551.1 EMBL· GenBank· DDBJ | mRNA | ||
AK316535 EMBL· GenBank· DDBJ | BAH14906.1 EMBL· GenBank· DDBJ | mRNA | ||
AF458593 EMBL· GenBank· DDBJ | AAM49721.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
BC018311 EMBL· GenBank· DDBJ | AAH18311.2 EMBL· GenBank· DDBJ | mRNA | ||
BC021551 EMBL· GenBank· DDBJ | AAH21551.2 EMBL· GenBank· DDBJ | mRNA | ||
BC068007 EMBL· GenBank· DDBJ | AAH68007.1 EMBL· GenBank· DDBJ | mRNA | ||
BC080628 EMBL· GenBank· DDBJ | AAH80628.1 EMBL· GenBank· DDBJ | mRNA | ||
BC101741 EMBL· GenBank· DDBJ | AAI01742.1 EMBL· GenBank· DDBJ | mRNA | ||
BC112182 EMBL· GenBank· DDBJ | AAI12183.1 EMBL· GenBank· DDBJ | mRNA |