Q5SXM2 · SNPC4_HUMAN

  • Protein
    snRNA-activating protein complex subunit 4
  • Gene
    SNAPC4
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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.

114692004006008001,0001,2001,400
TypeIDPosition(s)Description
DNA binding317-341H-T-H motif
DNA binding424-447H-T-H motif
DNA binding476-499H-T-H motif

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentnucleoplasm
Cellular Componentnucleus
Cellular ComponentsnRNA-activating protein complex
Molecular FunctionDNA binding
Molecular FunctionRNA polymerase II general transcription initiation factor activity
Molecular FunctionRNA polymerase III general transcription initiation factor activity
Molecular FunctionRNA polymerase III type 3 promoter sequence-specific DNA binding
Biological ProcesssnRNA transcription by RNA polymerase II
Biological ProcesssnRNA transcription by RNA polymerase III

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    snRNA-activating protein complex subunit 4
  • Short names
    SNAPc subunit 4
  • Alternative names
    • Proximal sequence element-binding transcription factor subunit alpha (PSE-binding factor subunit alpha; PTF subunit alpha)
    • snRNA-activating protein complex 190 kDa subunit (SNAPc 190 kDa subunit)

Gene names

    • Name
      SNAPC4
    • Synonyms
      SNAP190

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q5SXM2
  • Secondary accessions
    • Q9Y6P7

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Involvement in disease

Neurodevelopmental disorder with motor regression, progressive spastic paraplegia, and oromotor dysfunction (NEDRSO)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    An 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 also
    MIM:620515
Natural variants in NEDRSO
Variant IDPosition(s)ChangeDescription
VAR_089014185K>Ein NEDRSO; uncertain significance
VAR_089015199D>Nin NEDRSO; uncertain significance
VAR_089016386Q>Rin NEDRSO; uncertain significance
VAR_089017441D>Nin NEDRSO; uncertain significance
VAR_089018479I>Tin NEDRSO; uncertain significance
VAR_089019810-1469missingin NEDRSO; likely pathogenic
VAR_089020967G>Vin NEDRSO; uncertain significance

Features

Showing features for natural variant, mutagenesis.

TypeIDPosition(s)Description
Natural variantVAR_05945544in dbSNP:rs7031489
Mutagenesis94Abolishes SNAPC5 binding in the absence of SNAPC1. Minimal effect on SNAPC5 binding in the presence of SNAPC1.
Mutagenesis94Abolishes SNAPC5 binding in the absence of SNAPC1. Minimal effect on SNAPC5 binding in the presence of SNAPC1.
Mutagenesis115Abolishes SNAPC5 binding in the absence of SNAPC1. Minimal effect on SNAPC5 binding in the presence of SNAPC1.
Natural variantVAR_089014185in NEDRSO; uncertain significance
Natural variantVAR_089015199in NEDRSO; uncertain significance
Natural variantVAR_089016386in NEDRSO; uncertain significance
Natural variantVAR_089017441in NEDRSO; uncertain significance
Natural variantVAR_089018479in NEDRSO; uncertain significance
Natural variantVAR_050193799in dbSNP:rs3812571
Natural variantVAR_089019810-1469in NEDRSO; likely pathogenic
Natural variantVAR_089020967in NEDRSO; uncertain significance
Mutagenesis1314Abolishes SNAPC2-binding.
Mutagenesis1355Abolishes SNAPC2-binding.
Mutagenesis1362Abolishes SNAPC2-binding.
Mutagenesis1364Abolishes SNAPC2-binding.
Mutagenesis1369Decreased binding to SNAPC2.
Natural variantVAR_0501941448in dbSNP:rs3812561

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.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
ChainPRO_00001971201-1469UniProtsnRNA-activating protein complex subunit 4
Modified residue68UniProtPhosphoserine
Modified residue (large scale data)68PRIDEPhosphoserine
Modified residue (large scale data)597PRIDEPhosphoserine
Modified residue599UniProtPhosphoserine
Modified residue (large scale data)599PRIDEPhosphoserine
Modified residue (large scale data)625PRIDEPhosphothreonine
Modified residue626UniProtPhosphoserine
Modified residue (large scale data)626PRIDEPhosphoserine
Modified residue (large scale data)702PRIDEPhosphoserine
Modified residue1157UniProtPhosphothreonine
Modified residue (large scale data)1163PRIDEPhosphoserine
Modified residue (large scale data)1221PRIDEPhosphothreonine
Modified residue1224UniProtPhosphoserine
Modified residue (large scale data)1224PRIDEPhosphoserine
Modified residue1398UniProtPhosphoserine
Modified residue (large scale data)1398PRIDEPhosphoserine
Modified residue1400UniProtPhosphoserine
Modified residue (large scale data)1400PRIDEPhosphoserine
Modified residue (large scale data)1407PRIDEPhosphoserine
Modified residue1440UniProtPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

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

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q5SXM2SNAPC1 Q1653312EBI-2801093, EBI-11915024
BINARY Q5SXM2SNAPC5 O759713EBI-2801093, EBI-749483
View interactors in UniProtKB
View CPX-8637 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region16-82Disordered
Compositional bias28-42Polar residues
Compositional bias57-82Basic and acidic residues
Region84-133SNAPC5-binding
Domain250-288Myb-like 1
Domain289-343HTH myb-type 1
Domain344-395Myb-like 2
Domain396-451HTH myb-type 2
Domain452-503HTH myb-type 3
Compositional bias501-516Basic residues
Region501-558Disordered
Compositional bias517-546Polar residues
Region577-661Disordered
Compositional bias600-623Polar residues
Region685-710Disordered
Compositional bias834-881Polar residues
Region834-894Disordered
Region932-981Disordered
Compositional bias967-981Polar residues
Region1001-1051Disordered
Compositional bias1018-1032Polar residues
Region1121-1167Disordered
Compositional bias1126-1140Polar residues
Region1184-1266Disordered
Region1281-1393SNAPC2-binding
Compositional bias1430-1446Polar residues
Region1430-1449Disordered

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,469
  • Mass (Da)
    159,433
  • Last updated
    2004-12-21 v1
  • Checksum
    78CBCFB1887E106C
MDVDAEREKITQEIKELERILDPGSSGSHVEISESSLESDSEADSLPSEDLDPADPPISEEERWGEASNDEDDPKDKTLPEDPETCLQLNMVYQEVIQEKLAEANLLLAQNREQQEELMRDLAGSKGTKVKDGKSLPPSTYMGHFMKPYFKDKVTGVGPPANEDTREKAAQGIKAFEELLVTKWKNWEKALLRKSVVSDRLQRLLQPKLLKLEYLHQKQSKVSSELERQALEKQGREAEKEIQDINQLPEEALLGNRLDSHDWEKISNINFEGSRSAEEIRKFWQNSEHPSINKQEWSREEEERLQAIAAAHGHLEWQKIAEELGTSRSAFQCLQKFQQHNKALKRKEWTEEEDRMLTQLVQEMRVGSHIPYRRIVYYMEGRDSMQLIYRWTKSLDPGLKKGYWAPEEDAKLLQAVAKYGEQDWFKIREEVPGRSDAQCRDRYLRRLHFSLKKGRWNLKEEEQLIELIEKYGVGHWAKIASELPHRSGSQCLSKWKIMMGKKQGLRRRRRRARHSVRWSSTSSSGSSSGSSGGSSSSSSSSSEEDEPEQAQAGEGDRALLSPQYMVPDMDLWVPARQSTSQPWRGGAGAWLGGPAASLSPPKGSSASQGGSKEASTTAAAPGEETSPVQVPARAHGPVPRSAQASHSADTRPAGAEKQALEGGRRLLTVPVETVLRVLRANTAARSCTQKEQLRQPPLPTSSPGVSSGDSVARSHVQWLRHRATQSGQRRWRHALHRRLLNRRLLLAVTPWVGDVVVPCTQASQRPAVVQTQADGLREQLQQARLASTPVFTLFTQLFHIDTAGCLEVVRERKALPPRLPQAGARDPPVHLLQASSSAQSTPGHLFPNVPAQEASKSASHKGSRRLASSRVERTLPQASLLASTGPRPKPKTVSELLQEKRLQEARAREATRGPVVLPSQLLVSSSVILQPPLPHTPHGRPAPGPTVLNVPLSGPGAPAAAKPGTSGSWQEAGTSAKDKRLSTMQALPLAPVFSEAEGTAPAASQAPALGPGQISVSCPESGLGQSQAPAASRKQGLPEAPPFLPAAPSPTPLPVQPLSLTHIGGPHVATSVPLPVTWVLTAQGLLPVPVPAVVSLPRPAGTPGPAGLLATLLPPLTETRAAQGPRAPALSSSWQPPANMNREPEPSCRTDTPAPPTHALSQSPAEADGSVAFVPGEAQVAREIPEPRTSSHADPPEAEPPWSGRLPAFGGVIPATEPRGTPGSPSGTQEPRGPLGLEKLPLRQPGPEKGALDLEKPPLPQPGPEKGALDLGLLSQEGEAATQQWLGGQRGVRVPLLGSRLPYQPPALCSLRALSGLLLHKKALEHKATSLVVGGEAERPAGALQASLGLVRGQLQDNPAYLLLRARFLAAFTLPALLATLAPQGVRTTLSVPSRVGSESEDEDLLSELELADRDGQPGCTTATCPIQGAPDSGKCSASSCLDTSNDPDDLDVLRTRHARHTRKRRRLV

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8I5QKS3A0A8I5QKS3_HUMANSNAPC4286
A0A1B0GUB4A0A1B0GUB4_HUMANSNAPC4451

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias28-42Polar residues
Compositional bias57-82Basic and acidic residues
Compositional bias501-516Basic residues
Compositional bias517-546Polar residues
Compositional bias600-623Polar residues
Compositional bias834-881Polar residues
Compositional bias967-981Polar residues
Compositional bias1018-1032Polar residues
Sequence conflict1046in Ref. 1; AAC02972
Compositional bias1126-1140Polar residues
Compositional bias1430-1446Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF032387
EMBL· GenBank· DDBJ
AAC02972.1
EMBL· GenBank· DDBJ
mRNA
AL592301
EMBL· GenBank· DDBJ
CAI13935.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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