Q5SXM2 · SNPC4_HUMAN
- ProteinsnRNA-activating protein complex subunit 4
- GeneSNAPC4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1469 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Part of the SNAPc complex required for the transcription of both RNA polymerase II and III small-nuclear RNA genes. Binds to the proximal sequence element (PSE), a non-TATA-box basal promoter element common to these 2 types of genes. Recruits TBP and BRF2 to the U6 snRNA TATA box.
Features
Showing features for dna binding.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
DNA binding | 317-341 | H-T-H motif | ||||
Sequence: WQKIAEELGTSRSAFQCLQKFQQHN | ||||||
DNA binding | 424-447 | H-T-H motif | ||||
Sequence: WFKIREEVPGRSDAQCRDRYLRRL | ||||||
DNA binding | 476-499 | H-T-H motif | ||||
Sequence: WAKIASELPHRSGSQCLSKWKIMM |
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 | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | snRNA-activating protein complex | |
Molecular Function | DNA binding | |
Molecular Function | RNA polymerase II general transcription initiation factor activity | |
Molecular Function | RNA polymerase III general transcription initiation factor activity | |
Molecular Function | RNA polymerase III type 3 promoter sequence-specific DNA binding | |
Biological Process | snRNA transcription by RNA polymerase II | |
Biological Process | snRNA transcription by RNA polymerase III |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namesnRNA-activating protein complex subunit 4
- Short namesSNAPc subunit 4
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ5SXM2
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Neurodevelopmental disorder with motor regression, progressive spastic paraplegia, and oromotor dysfunction (NEDRSO)
- Note
- DescriptionAn autosomal recessive disorder characterized by delayed motor development and developmental regression after the first year of life, followed by progressive spasticity with gait alterations, paraparesis, and oromotor dysfunction. Most individuals have cerebral, cerebellar, or basal ganglia volume loss.
- See alsoMIM:620515
Natural variants in NEDRSO
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_089014 | 185 | K>E | in NEDRSO; uncertain significance | |
VAR_089015 | 199 | D>N | in NEDRSO; uncertain significance | |
VAR_089016 | 386 | Q>R | in NEDRSO; uncertain significance | |
VAR_089017 | 441 | D>N | in NEDRSO; uncertain significance | |
VAR_089018 | 479 | I>T | in NEDRSO; uncertain significance | |
VAR_089019 | 810-1469 | missing | in NEDRSO; likely pathogenic | |
VAR_089020 | 967 | G>V | in NEDRSO; uncertain significance |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_059455 | 44 | in dbSNP:rs7031489 | |||
Sequence: D → N | ||||||
Mutagenesis | 94 | Abolishes SNAPC5 binding in the absence of SNAPC1. Minimal effect on SNAPC5 binding in the presence of SNAPC1. | ||||
Sequence: Q → A | ||||||
Mutagenesis | 94 | Abolishes SNAPC5 binding in the absence of SNAPC1. Minimal effect on SNAPC5 binding in the presence of SNAPC1. | ||||
Sequence: Q → L | ||||||
Mutagenesis | 115 | Abolishes SNAPC5 binding in the absence of SNAPC1. Minimal effect on SNAPC5 binding in the presence of SNAPC1. | ||||
Sequence: Q → L | ||||||
Natural variant | VAR_089014 | 185 | in NEDRSO; uncertain significance | |||
Sequence: K → E | ||||||
Natural variant | VAR_089015 | 199 | in NEDRSO; uncertain significance | |||
Sequence: D → N | ||||||
Natural variant | VAR_089016 | 386 | in NEDRSO; uncertain significance | |||
Sequence: Q → R | ||||||
Natural variant | VAR_089017 | 441 | in NEDRSO; uncertain significance | |||
Sequence: D → N | ||||||
Natural variant | VAR_089018 | 479 | in NEDRSO; uncertain significance | |||
Sequence: I → T | ||||||
Natural variant | VAR_050193 | 799 | in dbSNP:rs3812571 | |||
Sequence: H → Q | ||||||
Natural variant | VAR_089019 | 810-1469 | in NEDRSO; likely pathogenic | |||
Sequence: Missing | ||||||
Natural variant | VAR_089020 | 967 | in NEDRSO; uncertain significance | |||
Sequence: G → V | ||||||
Mutagenesis | 1314 | Abolishes SNAPC2-binding. | ||||
Sequence: L → A | ||||||
Mutagenesis | 1355 | Abolishes SNAPC2-binding. | ||||
Sequence: L → A | ||||||
Mutagenesis | 1362 | Abolishes SNAPC2-binding. | ||||
Sequence: L → A | ||||||
Mutagenesis | 1364 | Abolishes SNAPC2-binding. | ||||
Sequence: L → A | ||||||
Mutagenesis | 1369 | Decreased binding to SNAPC2. | ||||
Sequence: L → A | ||||||
Natural variant | VAR_050194 | 1448 | in dbSNP:rs3812561 | |||
Sequence: P → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2,010 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
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_0000197120 | 1-1469 | UniProt | snRNA-activating protein complex subunit 4 | |||
Sequence: MDVDAEREKITQEIKELERILDPGSSGSHVEISESSLESDSEADSLPSEDLDPADPPISEEERWGEASNDEDDPKDKTLPEDPETCLQLNMVYQEVIQEKLAEANLLLAQNREQQEELMRDLAGSKGTKVKDGKSLPPSTYMGHFMKPYFKDKVTGVGPPANEDTREKAAQGIKAFEELLVTKWKNWEKALLRKSVVSDRLQRLLQPKLLKLEYLHQKQSKVSSELERQALEKQGREAEKEIQDINQLPEEALLGNRLDSHDWEKISNINFEGSRSAEEIRKFWQNSEHPSINKQEWSREEEERLQAIAAAHGHLEWQKIAEELGTSRSAFQCLQKFQQHNKALKRKEWTEEEDRMLTQLVQEMRVGSHIPYRRIVYYMEGRDSMQLIYRWTKSLDPGLKKGYWAPEEDAKLLQAVAKYGEQDWFKIREEVPGRSDAQCRDRYLRRLHFSLKKGRWNLKEEEQLIELIEKYGVGHWAKIASELPHRSGSQCLSKWKIMMGKKQGLRRRRRRARHSVRWSSTSSSGSSSGSSGGSSSSSSSSSEEDEPEQAQAGEGDRALLSPQYMVPDMDLWVPARQSTSQPWRGGAGAWLGGPAASLSPPKGSSASQGGSKEASTTAAAPGEETSPVQVPARAHGPVPRSAQASHSADTRPAGAEKQALEGGRRLLTVPVETVLRVLRANTAARSCTQKEQLRQPPLPTSSPGVSSGDSVARSHVQWLRHRATQSGQRRWRHALHRRLLNRRLLLAVTPWVGDVVVPCTQASQRPAVVQTQADGLREQLQQARLASTPVFTLFTQLFHIDTAGCLEVVRERKALPPRLPQAGARDPPVHLLQASSSAQSTPGHLFPNVPAQEASKSASHKGSRRLASSRVERTLPQASLLASTGPRPKPKTVSELLQEKRLQEARAREATRGPVVLPSQLLVSSSVILQPPLPHTPHGRPAPGPTVLNVPLSGPGAPAAAKPGTSGSWQEAGTSAKDKRLSTMQALPLAPVFSEAEGTAPAASQAPALGPGQISVSCPESGLGQSQAPAASRKQGLPEAPPFLPAAPSPTPLPVQPLSLTHIGGPHVATSVPLPVTWVLTAQGLLPVPVPAVVSLPRPAGTPGPAGLLATLLPPLTETRAAQGPRAPALSSSWQPPANMNREPEPSCRTDTPAPPTHALSQSPAEADGSVAFVPGEAQVAREIPEPRTSSHADPPEAEPPWSGRLPAFGGVIPATEPRGTPGSPSGTQEPRGPLGLEKLPLRQPGPEKGALDLEKPPLPQPGPEKGALDLGLLSQEGEAATQQWLGGQRGVRVPLLGSRLPYQPPALCSLRALSGLLLHKKALEHKATSLVVGGEAERPAGALQASLGLVRGQLQDNPAYLLLRARFLAAFTLPALLATLAPQGVRTTLSVPSRVGSESEDEDLLSELELADRDGQPGCTTATCPIQGAPDSGKCSASSCLDTSNDPDDLDVLRTRHARHTRKRRRLV | |||||||
Modified residue | 68 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 68 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 597 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 599 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 599 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 625 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 626 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 626 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 702 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1157 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1163 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1221 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1224 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1224 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1398 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1398 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1400 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1400 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1407 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1440 | UniProt | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Part of the SNAPc complex composed of 5 subunits: SNAPC1, SNAPC2, SNAPC3, SNAPC4 and SNAPC5. SNAPC4 interacts with SNAPC1, SNAPC2, SNAPC5, BRF2 and TBP.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q5SXM2 | SNAPC1 Q16533 | 12 | EBI-2801093, EBI-11915024 | |
BINARY | Q5SXM2 | SNAPC5 O75971 | 3 | EBI-2801093, EBI-749483 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 16-82 | Disordered | ||||
Sequence: ELERILDPGSSGSHVEISESSLESDSEADSLPSEDLDPADPPISEEERWGEASNDEDDPKDKTLPED | ||||||
Compositional bias | 28-42 | Polar residues | ||||
Sequence: SHVEISESSLESDSE | ||||||
Compositional bias | 57-82 | Basic and acidic residues | ||||
Sequence: PISEEERWGEASNDEDDPKDKTLPED | ||||||
Region | 84-133 | SNAPC5-binding | ||||
Sequence: ETCLQLNMVYQEVIQEKLAEANLLLAQNREQQEELMRDLAGSKGTKVKDG | ||||||
Domain | 250-288 | Myb-like 1 | ||||
Sequence: EEALLGNRLDSHDWEKISNINFEGSRSAEEIRKFWQNSE | ||||||
Domain | 289-343 | HTH myb-type 1 | ||||
Sequence: HPSINKQEWSREEEERLQAIAAAHGHLEWQKIAEELGTSRSAFQCLQKFQQHNKA | ||||||
Domain | 344-395 | Myb-like 2 | ||||
Sequence: LKRKEWTEEEDRMLTQLVQEMRVGSHIPYRRIVYYMEGRDSMQLIYRWTKSL | ||||||
Domain | 396-451 | HTH myb-type 2 | ||||
Sequence: DPGLKKGYWAPEEDAKLLQAVAKYGEQDWFKIREEVPGRSDAQCRDRYLRRLHFSL | ||||||
Domain | 452-503 | HTH myb-type 3 | ||||
Sequence: KKGRWNLKEEEQLIELIEKYGVGHWAKIASELPHRSGSQCLSKWKIMMGKKQ | ||||||
Compositional bias | 501-516 | Basic residues | ||||
Sequence: KKQGLRRRRRRARHSV | ||||||
Region | 501-558 | Disordered | ||||
Sequence: KKQGLRRRRRRARHSVRWSSTSSSGSSSGSSGGSSSSSSSSSEEDEPEQAQAGEGDRA | ||||||
Compositional bias | 517-546 | Polar residues | ||||
Sequence: RWSSTSSSGSSSGSSGGSSSSSSSSSEEDE | ||||||
Region | 577-661 | Disordered | ||||
Sequence: QSTSQPWRGGAGAWLGGPAASLSPPKGSSASQGGSKEASTTAAAPGEETSPVQVPARAHGPVPRSAQASHSADTRPAGAEKQALE | ||||||
Compositional bias | 600-623 | Polar residues | ||||
Sequence: PPKGSSASQGGSKEASTTAAAPGE | ||||||
Region | 685-710 | Disordered | ||||
Sequence: RSCTQKEQLRQPPLPTSSPGVSSGDS | ||||||
Compositional bias | 834-881 | Polar residues | ||||
Sequence: ASSSAQSTPGHLFPNVPAQEASKSASHKGSRRLASSRVERTLPQASLL | ||||||
Region | 834-894 | Disordered | ||||
Sequence: ASSSAQSTPGHLFPNVPAQEASKSASHKGSRRLASSRVERTLPQASLLASTGPRPKPKTVS | ||||||
Region | 932-981 | Disordered | ||||
Sequence: PLPHTPHGRPAPGPTVLNVPLSGPGAPAAAKPGTSGSWQEAGTSAKDKRL | ||||||
Compositional bias | 967-981 | Polar residues | ||||
Sequence: GSWQEAGTSAKDKRL | ||||||
Region | 1001-1051 | Disordered | ||||
Sequence: PAASQAPALGPGQISVSCPESGLGQSQAPAASRKQGLPEAPPFLPAAPSPT | ||||||
Compositional bias | 1018-1032 | Polar residues | ||||
Sequence: CPESGLGQSQAPAAS | ||||||
Region | 1121-1167 | Disordered | ||||
Sequence: AAQGPRAPALSSSWQPPANMNREPEPSCRTDTPAPPTHALSQSPAEA | ||||||
Compositional bias | 1126-1140 | Polar residues | ||||
Sequence: RAPALSSSWQPPANM | ||||||
Region | 1184-1266 | Disordered | ||||
Sequence: IPEPRTSSHADPPEAEPPWSGRLPAFGGVIPATEPRGTPGSPSGTQEPRGPLGLEKLPLRQPGPEKGALDLEKPPLPQPGPEK | ||||||
Region | 1281-1393 | SNAPC2-binding | ||||
Sequence: ATQQWLGGQRGVRVPLLGSRLPYQPPALCSLRALSGLLLHKKALEHKATSLVVGGEAERPAGALQASLGLVRGQLQDNPAYLLLRARFLAAFTLPALLATLAPQGVRTTLSVP | ||||||
Compositional bias | 1430-1446 | Polar residues | ||||
Sequence: APDSGKCSASSCLDTSN | ||||||
Region | 1430-1449 | Disordered | ||||
Sequence: APDSGKCSASSCLDTSNDPD |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,469
- Mass (Da)159,433
- Last updated2004-12-21 v1
- Checksum78CBCFB1887E106C
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I5QKS3 | A0A8I5QKS3_HUMAN | SNAPC4 | 286 | ||
A0A1B0GUB4 | A0A1B0GUB4_HUMAN | SNAPC4 | 451 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 28-42 | Polar residues | ||||
Sequence: SHVEISESSLESDSE | ||||||
Compositional bias | 57-82 | Basic and acidic residues | ||||
Sequence: PISEEERWGEASNDEDDPKDKTLPED | ||||||
Compositional bias | 501-516 | Basic residues | ||||
Sequence: KKQGLRRRRRRARHSV | ||||||
Compositional bias | 517-546 | Polar residues | ||||
Sequence: RWSSTSSSGSSSGSSGGSSSSSSSSSEEDE | ||||||
Compositional bias | 600-623 | Polar residues | ||||
Sequence: PPKGSSASQGGSKEASTTAAAPGE | ||||||
Compositional bias | 834-881 | Polar residues | ||||
Sequence: ASSSAQSTPGHLFPNVPAQEASKSASHKGSRRLASSRVERTLPQASLL | ||||||
Compositional bias | 967-981 | Polar residues | ||||
Sequence: GSWQEAGTSAKDKRL | ||||||
Compositional bias | 1018-1032 | Polar residues | ||||
Sequence: CPESGLGQSQAPAAS | ||||||
Sequence conflict | 1046 | in Ref. 1; AAC02972 | ||||
Sequence: A → G | ||||||
Compositional bias | 1126-1140 | Polar residues | ||||
Sequence: RAPALSSSWQPPANM | ||||||
Compositional bias | 1430-1446 | Polar residues | ||||
Sequence: APDSGKCSASSCLDTSN |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF032387 EMBL· GenBank· DDBJ | AAC02972.1 EMBL· GenBank· DDBJ | mRNA | ||
AL592301 EMBL· GenBank· DDBJ | CAI13935.1 EMBL· GenBank· DDBJ | Genomic DNA |