Seroatlas · Human Serome Atlas

SNRNP200

U5 small nuclear ribonucleoprotein 200 kDa helicase

Also known as: ASCC3L1, BRR2, HELIC2, KIAA0788, RP33, U5-200KD, U520_HUMAN

Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene

Protein identityUniProt · HPA

UniProt accession
O75643
Gene
SNRNP200
Ensembl
ENSG00000144028
Chromosome
2
Canonical length
2136 aa
Protein class
Disease related genes, Enzymes, Human disease related genes, Plasma proteins, Potential drug targets, Predicted intracellular proteins
Subcellular location
Nucleoplasm,Primary cilium

OverviewNCBI Gene

Pre-mRNA splicing is catalyzed by the spliceosome, a complex of specialized RNA and protein subunits that removes introns from a transcribed pre-mRNA segment. The spliceosome consists of small nuclear RNA proteins (snRNPs) U1, U2, U4, U5 and U6, together with approximately 80 conserved proteins. U5 snRNP contains nine specific proteins. This gene encodes one of the U5 snRNP-specific proteins. This protein belongs to the DEXH-box family of putative RNA helicases. It is a core component of U4/U6-U5 snRNPs and appears to catalyze an ATP-dependent unwinding of U4/U6 RNA duplices. Mutations in this gene cause autosomal-dominant retinitis pigmentosa. Alternatively spliced transcript variants encoding different isoforms have been found, but the full-length nature of these variants has not been determined. [provided by RefSeq, Mar 2010]

Canonical amino-acid sequenceUniProt

2136 residues, UniProt reviewed canonical sequence.

>O75643|SNRNP200
     1  MADVTARSLQ YEYKANSNLV LQADRSLIDR TRRDEPTGEV LSLVGKLEGT RMGDKAQRTK
    61  PQMQEERRAK RRKRDEDRHD INKMKGYTLL SEGIDEMVGI IYKPKTKETR ETYEVLLSFI
   121  QAALGDQPRD ILCGAADEVL AVLKNEKLRD KERRKEIDLL LGQTDDTRYH VLVNLGKKIT
   181  DYGGDKEIQN MDDNIDETYG VNVQFESDEE EGDEDVYGEV REEASDDDME GDEAVVRCTL
   241  SANLVASGEL MSSKKKDLHP RDIDAFWLQR QLSRFYDDAI VSQKKADEVL EILKTASDDR
   301  ECENQLVLLL GFNTFDFIKV LRQHRMMILY CTLLASAQSE AEKERIMGKM EADPELSKFL
   361  YQLHETEKED LIREERSRRE RVRQSRMDTD LETMDLDQGG EALAPRQVLD LEDLVFTQGS
   421  HFMANKRCQL PDGSFRRQRK GYEEVHVPAL KPKPFGSEEQ LLPVEKLPKY AQAGFEGFKT
   481  LNRIQSKLYR AALETDENLL LCAPTGAGKT NVALMCMLRE IGKHINMDGT INVDDFKIIY
   541  IAPMRSLVQE MVGSFGKRLA TYGITVAELT GDHQLCKEEI SATQIIVCTP EKWDIITRKG
   601  GERTYTQLVR LIILDEIHLL HDDRGPVLEA LVARAIRNIE MTQEDVRLIG LSATLPNYED
   661  VATFLRVDPA KGLFYFDNSF RPVPLEQTYV GITEKKAIKR FQIMNEIVYE KIMEHAGKNQ
   721  VLVFVHSRKE TGKTARAIRD MCLEKDTLGL FLREGSASTE VLRTEAEQCK NLELKDLLPY
   781  GFAIHHAGMT RVDRTLVEDL FADKHIQVLV STATLAWGVN LPAHTVIIKG TQVYSPEKGR
   841  WTELGALDIL QMLGRAGRPQ YDTKGEGILI TSHGELQYYL SLLNQQLPIE SQMVSKLPDM
   901  LNAEIVLGNV QNAKDAVNWL GYAYLYIRML RSPTLYGISH DDLKGDPLLD QRRLDLVHTA
   961  ALMLDKNNLV KYDKKTGNFQ VTELGRIASH YYITNDTVQT YNQLLKPTLS EIELFRVFSL
  1021  SSEFKNITVR EEEKLELQKL LERVPIPVKE SIEEPSAKIN VLLQAFISQL KLEGFALMAD
  1081  MVYVTQSAGR LMRAIFEIVL NRGWAQLTDK TLNLCKMIDK RMWQSMCPLR QFRKLPEEVV
  1141  KKIEKKNFPF ERLYDLNHNE IGELIRMPKM GKTIHKYVHL FPKLELSVHL QPITRSTLKV
  1201  ELTITPDFQW DEKVHGSSEA FWILVEDVDS EVILHHEYFL LKAKYAQDEH LITFFVPVFE
  1261  PLPPQYFIRV VSDRWLSCET QLPVSFRHLI LPEKYPPPTE LLDLQPLPVS ALRNSAFESL
  1321  YQDKFPFFNP IQTQVFNTVY NSDDNVFVGA PTGSGKTICA EFAILRMLLQ SSEGRCVYIT
  1381  PMEALAEQVY MDWYEKFQDR LNKKVVLLTG ETSTDLKLLG KGNIIISTPE KWDILSRRWK
  1441  QRKNVQNINL FVVDEVHLIG GENGPVLEVI CSRMRYISSQ IERPIRIVAL SSSLSNAKDV
  1501  AHWLGCSATS TFNFHPNVRP VPLELHIQGF NISHTQTRLL SMAKPVYHAI TKHSPKKPVI
  1561  VFVPSRKQTR LTAIDILTTC AADIQRQRFL HCTEKDLIPY LEKLSDSTLK ETLLNGVGYL
  1621  HEGLSPMERR LVEQLFSSGA IQVVVASRSL CWGMNVAAHL VIIMDTQYYN GKIHAYVDYP
  1681  IYDVLQMVGH ANRPLQDDEG RCVIMCQGSK KDFFKKFLYE PLPVESHLDH CMHDHFNAEI
  1741  VTKTIENKQD AVDYLTWTFL YRRMTQNPNY YNLQGISHRH LSDHLSELVE QTLSDLEQSK
  1801  CISIEDEMDV APLNLGMIAA YYYINYTTIE LFSMSLNAKT KVRGLIEIIS NAAEYENIPI
  1861  RHHEDNLLRQ LAQKVPHKLN NPKFNDPHVK TNLLLQAHLS RMQLSAELQS DTEEILSKAI
  1921  RLIQACVDVL SSNGWLSPAL AAMELAQMVT QAMWSKDSYL KQLPHFTSEH IKRCTDKGVE
  1981  SVFDIMEMED EERNALLQLT DSQIADVARF CNRYPNIELS YEVVDKDSIR SGGPVVVLVQ
  2041  LEREEEVTGP VIAPLFPQKR EEGWWVVIGD AKSNSLISIK RLTLQQKAKV KLDFVAPATG
  2101  AHNYTLYFMS DAYMGCDQEY KFSVDVKEAE TDSDSD

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against SNRNP200 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability
Intracellular
Secreted
No
Transmembrane segments
0
Mean surface accessibility (rSASA)
0.27
Highest tissue expression
69 nTPM

Expression across tissuesHPA

Tissue

  • thymus: 69 nTPM
  • retina: 63 nTPM
  • bone marrow: 56 nTPM
  • parathyroid gland: 49 nTPM
  • tonsil: 49 nTPM
  • skeletal muscle: 44 nTPM

Single-cell type

  • erythrocyte progenitors: 148 nCPM
  • lacrimal acinar cells: 100 nCPM
  • rod photoreceptor cells: 99 nCPM
  • t-cells: 95 nCPM
  • early primary spermatocytes: 95 nCPM
  • müller glia: 94 nCPM

Immune cell

  • basophil: 17 nTPM
  • memory CD8 T-cell: 9.5 nTPM
  • MAIT T-cell: 9 nTPM
  • gdT-cell: 7.9 nTPM
  • NK-cell: 7.3 nTPM
  • naive CD8 T-cell: 7.1 nTPM

Brain region

  • choroid plexus: 75 nTPM
  • cerebellum: 56 nTPM
  • white matter: 51 nTPM
  • medulla oblongata: 49 nTPM
  • spinal cord: 47 nTPM
  • cerebral cortex: 46 nTPM

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about SNRNP200.

Disease | AllUniProt

Conditions SNRNP200 is implicated in, by any mechanism.

Disease | GeneticClinVar

17 pathogenic / likely-pathogenic of 1,467 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)
0.08
gnomAD pLI
1
gnomAD missense Z
5.94
DepMap mean gene effect
-2.32
DepMap dependency class
pan

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 6% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

Molecular functions

Cellular components

Protein domainsUniProt · Pfam · InterPro

KeywordsUniProt

InteractionsUniProt · HPA

Protein binding partners of SNRNP200 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

Antibody and autoantibody relevanceSeroatlas analysis

Seroatlas reads SNRNP200 as an antibody target. Whether an autoantibody or antibody against SNRNP200 could matter depends on whether native SNRNP200 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.

SNRNP200 is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.

Annotation status

The present source text does not explicitly label SNRNP200 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.

Canonical record: https://seroatlas.com/gene/SNRNP200. Study-independent annotations aggregated from UniProt, Human Protein Atlas, PubMed, IEDB, Pfam, InterPro, Gene Ontology, AlphaFold, gnomAD, DepMap, ClinVar, TCGA. Catalog release seroatlas-reviewed-human-uniprot-20260313.

Seroatlas is the reference for exploring autoantibody and antibody serology at the human-protein level: the autoreactome and human serome, multiplex serology (HuProt, HuScan, VirScan, PhIP-Seq).

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