Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q13702 (RAPSN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
43 kDa receptor-associated protein of the synapse

Short name=RAPsyn
Alternative name(s):
43 kDa postsynaptic protein
Acetylcholine receptor-associated 43 kDa protein
RING finger protein 205
Gene names
Name:RAPSN
Synonyms:RNF205
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length412 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Postsynaptic protein required for clustering of nicotinic acetylcholine receptors (nAChRs) at the neuromuscular junction. It may link the receptor to the underlying postsynaptic cytoskeleton, possibly by direct association with actin or spectrin.

Subcellular location

Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junctionsynapsepostsynaptic cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcytoskeleton. Note: Cytoplasmic surface of postsynaptic membranes.

Domain

A cysteine-rich region homologous to part of the regulatory domain of protein kinase C may be important in interactions of this protein with the lipid bilayer.

Post-translational modification

Ubiquitinated by the BCR(KLHL8) complex, leading to its degradation. Ref.5

Involvement in disease

Myasthenic syndrome, congenital, associated with acetylcholine receptor deficiency (CMS-ACHRD) [MIM:608931]: A post-synaptic congenital myasthenic syndrome. Congenital myasthenic syndromes (CMS) are inherited disorders of neuromuscular transmission that stem from mutations in presynaptic, synaptic, or postsynaptic proteins.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Fetal akinesia deformation sequence (FADS) [MIM:208150]: Rare condition characterized by decreased intrauterine fetal movement, congenital limb contractures, pulmonary hypoplasia, polyhydramnios and craniofacial abnormalities.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14 Ref.15

Sequence similarities

Belongs to the RAPsyn family.

Contains 1 RING-type zinc finger.

Contains 7 TPR repeats.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13702-1)

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.
Isoform 2 (identifier: Q13702-2)

The sequence of this isoform differs from the canonical sequence as follows:
     264-322: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 41241143 kDa receptor-associated protein of the synapse
PRO_0000167591

Regions

Repeat6 – 3934TPR 1
Repeat83 – 11634TPR 2
Repeat123 – 15634TPR 3
Repeat163 – 19634TPR 4
Repeat206 – 23934TPR 5
Repeat246 – 27934TPR 6
Repeat286 – 31934TPR 7
Zinc finger363 – 40341RING-type

Amino acid modifications

Modified residue1961Phosphotyrosine Potential
Modified residue4051Phosphoserine Potential
Lipidation21N-myristoyl glycine By similarity

Natural variations

Alternative sequence264 – 32259Missing in isoform 2.
VSP_005533
Natural variant81Q → K. Ref.4
Corresponds to variant rs11556408 [ dbSNP | Ensembl ].
VAR_043897
Natural variant141L → P in CMS-ACHRD. Ref.2 Ref.6 Ref.7
VAR_021216
Natural variant451V → M in CMS-ACHRD; reduced coclustering with acetylcholine receptor. Ref.13
VAR_043898
Natural variant811F → L.
Corresponds to variant rs57878668 [ dbSNP | Ensembl ].
VAR_062142
Natural variant881N → K in CMS-ACHRD. Ref.2 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11
Corresponds to variant rs104894299 [ dbSNP | Ensembl ].
VAR_021217
Natural variant1391F → S in FADS. Ref.15
VAR_043899
Natural variant1621E → K in CMS-ACHRD; reduced coclustering with acetylcholine receptor. Ref.13
VAR_043900
Natural variant1641R → C in CMS-ACHRD; reduced coclustering with acetylcholine receptor. Ref.12
VAR_043901
Natural variant1891A → V in FADS. Ref.15
VAR_043902
Natural variant2831L → P in CMS-ACHRD; reduced coclustering with acetylcholine receptor. Ref.12
VAR_043903

Experimental info

Sequence conflict1121L → V in CAA83954. Ref.1
Sequence conflict1591A → T in CAA83954. Ref.1
Sequence conflict2051R → Q in CAA83954. Ref.1
Sequence conflict3641G → A in CAA83954. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 17, 2007. Version 4.
Checksum: D17AC566700F5AAF

FASTA41246,328
        10         20         30         40         50         60 
MGQDQTKQQI EKGLQLYQSN QTEKALQVWT KVLEKSSDLM GRFRVLGCLV TAHSEMGRYK 

        70         80         90        100        110        120 
EMLKFAVVQI DTARELEDAD FLLESYLNLA RSNEKLCEFH KTISYCKTCL GLPGTRAGAQ 

       130        140        150        160        170        180 
LGGQVSLSMG NAFLGLSVFQ KALESFEKAL RYAHNNDDAM LECRVCCSLG SFYAQVKDYE 

       190        200        210        220        230        240 
KALFFPCKAA ELVNNYGKGW SLKYRAMSQY HMAVAYRLLG RLGSAMECCE ESMKIALQHG 

       250        260        270        280        290        300 
DRPLQALCLL CFADIHRSRG DLETAFPRYD SAMSIMTEIG NRLGQVQALL GVAKCWVARK 

       310        320        330        340        350        360 
ALDKALDAIE RAQDLAEEVG NKLSQLKLHC LSESIYRSKG LQRELRAHVV RFHECVEETE 

       370        380        390        400        410 
LYCGLCGESI GEKNSRLQAL PCSHIFHLRC LQNNGTRSCP NCRRSSMKPG FV 

« Hide

Isoform 2 [UniParc].

Checksum: 79A95D25A1FAA69A
Show »

FASTA35339,912

References

« Hide 'large scale' references
[1]"Cloning of cDNA encoding human rapsyn and mapping of the RAPSN gene locus to chromosome 11p11.2-p11.1."
Buckel A., Beeson D., James M., Vincent A.
Genomics 35:613-616(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Muscle.
[2]"Rapsyn mutations in humans cause endplate acetylcholine-receptor deficiency and myasthenic syndrome."
Ohno K., Engel A.G., Shen X.-M., Selcen D., Brengman J., Harper C.M., Tsujino A., Milone M.
Am. J. Hum. Genet. 70:875-885(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS CMS-ACHRD PRO-14 AND LYS-88.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT LYS-8.
Tissue: Muscle.
[5]"Control of rapsyn stability by the CUL-3-containing E3 ligase complex."
Nam S., Min K., Hwang H., Lee H.O., Lee J.H., Yoon J., Lee H., Park S., Lee J.
J. Biol. Chem. 284:8195-8206(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION BY THE BCR(KLHL8) COMPLEX.
[6]"Identification of pathogenic mutations in the human rapsyn gene."
Dunne V., Maselli R.A.
J. Hum. Genet. 48:204-207(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CMS-ACHRD PRO-14 AND LYS-88.
[7]"Rapsyn mutations in myasthenic syndrome due to impaired receptor clustering."
Maselli R.A., Dunne V., Pascual-Pascual S.I., Bowe C., Agius M., Frank R., Wollmann R.L.
Muscle Nerve 28:293-301(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CMS-ACHRD PRO-14 AND LYS-88.
[8]"Rapsyn N88K is a frequent cause of congenital myasthenic syndromes in European patients."
Mueller J.S., Mildner G., Mueller-Felber W., Schara U., Krampfl K., Petersen B., Petrova S., Stucka R., Mortier W., Bufler J., Kurlemann G., Huebner A., Merlini L., Lochmuller H., Abicht A.
Neurology 60:1805-1810(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CMS-ACHRD LYS-88.
[9]"Rapsyn mutations in hereditary myasthenia: distinct early- and late-onset phenotypes."
Burke G., Cossins J., Maxwell S., Owens G., Vincent A., Robb S., Nicolle M., Hilton-Jones D., Newsom-Davis J., Palace J., Beeson D.
Neurology 61:826-828(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CMS-ACHRD LYS-88.
[10]"Novel truncating RAPSN mutations causing congenital myasthenic syndrome responsive to 3,4-diaminopyridine."
Banwell B.L., Ohno K., Sieb J.P., Engel A.G.
Neuromuscul. Disord. 14:202-207(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CMS-ACHRD LYS-88.
[11]"Congenital myasthenic syndrome due to rapsyn deficiency: three cases with arthrogryposis and bulbar symptoms."
Ioos C., Barois A., Richard P., Eymard B., Hantai D., Estournet-Mathiaud B.
Neuropediatrics 35:246-249(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CMS-ACHRD LYS-88.
[12]"Impaired receptor clustering in congenital myasthenic syndrome with novel RAPSN mutations."
Mueller J.S., Baumeister S.K., Rasic V.M., Krause S., Todorovic S., Kugler K., Mueller-Felber W., Abicht A., Lochmueller H.
Neurology 67:1159-1164(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CMS-ACHRD CYS-164 AND PRO-283, CHARACTERIZATION OF VARIANTS CMS-ACHRD CYS-164 AND PRO-283.
[13]"Congenital myasthenic syndrome caused by two non-N88K rapsyn mutations."
Maselli R.A., Dris H., Schnier J., Cockrell J.L., Wollmann R.L.
Clin. Genet. 72:63-65(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CMS-ACHRD MET-45 AND LYS-162, CHARACTERIZATION OF VARIANTS CMS-ACHRD MET-45 AND LYS-162.
[14]"Mutation analysis of CHRNA1, CHRNB1, CHRND, and RAPSN genes in multiple pterygium syndrome/fetal akinesia patients."
Vogt J., Harrison B.J., Spearman H., Cossins J., Vermeer S., ten Cate L.N., Morgan N.V., Beeson D., Maher E.R.
Am. J. Hum. Genet. 82:222-227(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN FADS.
[15]"Acetylcholine receptor pathway mutations explain various fetal akinesia deformation sequence disorders."
Michalk A., Stricker S., Becker J., Rupps R., Pantzar T., Miertus J., Botta G., Naretto V.G., Janetzki C., Yaqoob N., Ott C.-E., Seelow D., Wieczorek D., Fiebig B., Wirth B., Hoopmann M., Walther M., Koerber F. expand/collapse author list , Blankenburg M., Mundlos S., Heller R., Hoffmann K.
Am. J. Hum. Genet. 82:464-476(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FADS SER-139 AND VAL-189.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z33905 mRNA. Translation: CAA83954.1.
AF449218 mRNA. Translation: AAL86639.1.
CH471064 Genomic DNA. Translation: EAW67914.1.
BC004196 mRNA. Translation: AAH04196.1.
PIRS45064.
RefSeqNP_005046.2. NM_005055.4.
NP_116034.2. NM_032645.4.
UniGeneHs.81218.

3D structure databases

ProteinModelPortalQ13702.
SMRQ13702. Positions 18-326.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111848. 5 interactions.
IntActQ13702. 2 interactions.
STRING9606.ENSP00000298854.

Chemistry

ChEMBLCHEMBL2163166.

PTM databases

PhosphoSiteQ13702.

Polymorphism databases

DMDM145559521.

Proteomic databases

PaxDbQ13702.
PRIDEQ13702.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000298854; ENSP00000298854; ENSG00000165917. [Q13702-1]
ENST00000352508; ENSP00000298853; ENSG00000165917. [Q13702-2]
GeneID5913.
KEGGhsa:5913.
UCSCuc001nfi.2. human. [Q13702-1]
uc001nfj.2. human. [Q13702-2]

Organism-specific databases

CTD5913.
GeneCardsGC11M047459.
HGNCHGNC:9863. RAPSN.
HPAHPA039475.
MIM208150. phenotype.
601592. gene.
608931. phenotype.
neXtProtNX_Q13702.
Orphanet994. Fetal akinesia deformation sequence.
33108. Lethal multiple pterygium syndrome.
98913. Postsynaptic congenital myasthenic syndromes.
PharmGKBPA34224.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0457.
HOGENOMHOG000231395.
HOVERGENHBG061484.
InParanoidQ13702.
OMAEEMELYC.
PhylomeDBQ13702.
TreeFamTF328344.

Gene expression databases

ArrayExpressQ13702.
BgeeQ13702.
CleanExHS_RAPSN.
GenevestigatorQ13702.

Family and domain databases

Gene3D1.25.40.10. 2 hits.
3.30.40.10. 1 hit.
InterProIPR001237. Postsynaptic.
IPR018293. Postsynaptic_CS.
IPR019568. Rapsyn_myristoylation/link_N.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERPTHR10098:SF16. PTHR10098:SF16. 1 hit.
PfamPF10579. Rapsyn_N. 1 hit.
PF00515. TPR_1. 1 hit.
PF13181. TPR_8. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view]
PRINTSPR00217. POSTSYNAPTIC.
SMARTSM00184. RING. 1 hit.
SM00028. TPR. 6 hits.
[Graphical view]
PROSITEPS00405. 43_KD_POSTSYNAPTIC. 1 hit.
PS50005. TPR. 5 hits.
PS50293. TPR_REGION. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRAPSN.
GenomeRNAi5913.
NextBio23012.
PROQ13702.
SOURCESearch...

Entry information

Entry nameRAPSN_HUMAN
AccessionPrimary (citable) accession number: Q13702
Secondary accession number(s): Q8TDF3, Q9BTD9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 17, 2007
Last modified: April 16, 2014
This is version 148 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM