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Table 2 COL5A1 and COL5A2 mutations in patients with cEDS

From: Clinical and molecular characterization of 40 patients with classic Ehlers–Danlos syndrome: identification of 18 COL5A1 and 2 COL5A2 novel mutations

Patient(s) IDs

Gene

Exon, intron/localization

aChange at the nucleotide level

bNonsense/Missense

bFrameshift

Splice site

Mutations leading to type V collagen haploinsufficiency

AN_002501

A1

ex1/N-propeptide

c.87G>A°

p.(Trp29*)

  

AN_002503-05#

A1

int7/N-propeptide

c.1165-2A>G

 

p.(Pro389Leufs*168)

c Activation of cryptic splice acceptor site 4 bp downstream of WT acceptor

AN_002506

A1

ex13/N-propeptide

c.1651C>T°

p.(Gln551*)

  

AN_002509

A1

int31/helix

c.2647-12A>G°

 

p.(Gly883Leufs*195)

c Creation of new splice acceptor site 11 bp upstream of WT acceptor

AN_002510

A1

ex34/helix

c.2757_2774del18insA°

 

p.(Glu920Hisfs*14)

 

AN_002511

A1

ex36/helix

c.2891dup°

 

p.(Gly967Trpfs*47)

 

AN_002514-15*

A1

ex38/helix

c.2988del°

 

p.(Gly997Alafs*77)

 

AN_002516

A1

ex38/helix

c.2988dup^ e

 

p.(Gly997Argfs*17)

 

AN_002517

A1

ex42/helix

c.3328C>T°

p.(Gln1110*)

  

AN_002520-23#

A1

ex45/helix

c.3568C>T

p.(Gln1190*)

  

AN_002524-25*

A1

ex48/helix

c.3769C>T° e

p.(Arg1257*)

  

AN_002527

A1

ex62/C-propeptide

c.4714del°

 

p.(Val1572Serfs*47)

 

AN_002528-29#

A1

ex62/C-propeptide

c.4919_4928del10^

 

p.(Lys1640Serfs*86)

 

AN_002530-31#

A1

ex63/C-propeptide

c.4962C>G

p.(Tyr1654*)

  

AN_002532

A1

ex66/C-propeptide

c.5458_5459del°

 

p.(Phe1820Argfs*2)

 

Large genomic rearrangement identified by MLPA and SNP-array

AN_002535-37#

A1

 

chr9.hg19:g.(137,440,166_137,442,686)_(137,633,699_137,638,368)dup

Mutations affecting the structural integrity of type V collagen

AN_002502

A1

ex4/N-propeptide

c.532A>C°

p.(Thr178Pro)

  

AN_002507-08#

A1

ex29/helix

c.2436A>T

p.(Glu812Asp)

 

c alteration of an ESE sequence, splice error?

AN_002512-13#

A1

int37/helix

c.2952+2_2952+3del

p.(Gly967_Thr984del)

 

c in-frame exon 37 skipping

AN_002518-19#

A1

ex43/helix

c.3413G>A e

p.(Gly1138Glu)

  

AN_002526

A1

ex54/helix

c.4178G>A°

p.(Gly1393Asp)

  

AN_002533

A2

ex29/helix

c.1977G>A°

p.(Gly642_Pro659del)

 

c in-frame exon 29 skipping

AN_002534

A2

int37/helix

c.2499+2T>C°

p.(Gly816_Pro833del)

 

d in-frame exon 37 skipping

  1. The patient(s) IDs correspond to the identifiers found in the LOVD EDS Variant Database (http://www.le.ac.uk/ge/collagen/); a DNA mutation numbering is based on the cDNA sequence. For cDNA numbering, +1 corresponds to the A of the ATG translation initiation codon in the reference sequence. The reference sequences are based on the GenBank Accession no.: COL5A1 NM_000093.3, COL5A2 NM_000393.3. b For protein numbering, +1 corresponds to the first translated amino acid. The reference sequences are based on GenBank Accession no.: COL5A1 NP_000084.3, COL5A2 NP_000384.2. c The effect on splicing was analyzed using four prediction programs (SpliceSite-Finder-like, MaxEntScan, NNSPLICE and Human Splicing Finder) in Alamut software, version 2.2 (Additional file 1: Figures S1–S6). d The effect on mRNA splicing was verified by RT-PCR of total RNA that was purified from the patient’s skin fibroblasts (Additional file 1: Figure S6B). ° de novo mutation verified by parental testing. ^ Parents not available for de novo testing. # Members of the same family. * Members of different families. e Mutation previously reported [18, LOVD].
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Orphanet Journal of Rare Diseases

ISSN: 1750-1172