PMID- 10508838
OWN - NLM
STAT- MEDLINE
DCOM- 19991122
LR  - 20190607
IS  - 1088-9051 (Print)
IS  - 1088-9051 (Linking)
VI  - 9
IP  - 9
DP  - 1999 Sep
TI  - Duplications on human chromosome 22 reveal a novel Ret Finger Protein-like gene
      family with sense and endogenous antisense transcripts.
PG  - 803-14
AB  - Analysis of 600 kb of sequence encompassing the beta-prime adaptin (BAM22) gene
      on human chromosome 22 revealed intrachromosomal duplications within 22q12-13
      resulting in three active RFPL genes, two RFPL pseudogenes, and two pseudogenes
      of BAM22. The genomic sequence of BAM22vartheta1 shows a remarkable similarity to
      that of BAM22. The cDNA sequence comparison of RFPL1, RFPL2, and RFPL3 showed
      95%-96% identity between the genes, which were most similar to the Ret Finger
      Protein gene from human chromosome 6. The sense RFPL transcripts encode proteins 
      with the tripartite structure, composed of RING finger, coiled-coil, and B30-2
      domains, which are characteristic of the RING-B30 family. Each of these domains
      are thought to mediate protein-protein interactions by promoting homo- or
      heterodimerization. The MID1 gene on Xp22 is also a member of the RING-B30 family
      and is mutated in Opitz syndrome (OS). The autosomal dominant form of OS shows
      linkage to 22q11-q12. We detected a polymorphic protein-truncating allele of
      RFPL1 in 8% of the population, which was not associated with the OS phenotype. We
      identified 6-kb and 1.2-kb noncoding antisense mRNAs of RFPL1S and RFPL3S
      antisense genes, respectively. The RFPL1S and RFPL3S genes cover substantial
      portions of their sense counterparts, which suggests that the function of RFPL1S 
      and RFPL3S is a post-transcriptional regulation of the sense RFPL genes. We
      illustrate the role of intrachromosomal duplications in the generation of RFPL
      genes, which were created by a series of duplications and share an ancestor with 
      the RING-B30 domain containing genes from the major histocompatibility complex
      region on human chromosome 6.
FAU - Seroussi, E
AU  - Seroussi E
AD  - Department of Molecular Medicine, Karolinska Hospital, 171 76 Stockholm, Sweden.
FAU - Kedra, D
AU  - Kedra D
FAU - Pan, H Q
AU  - Pan HQ
FAU - Peyrard, M
AU  - Peyrard M
FAU - Schwartz, C
AU  - Schwartz C
FAU - Scambler, P
AU  - Scambler P
FAU - Donnai, D
AU  - Donnai D
FAU - Roe, B A
AU  - Roe BA
FAU - Dumanski, J P
AU  - Dumanski JP
LA  - eng
SI  - GENBANK/AC000025
SI  - GENBANK/AC000041
SI  - GENBANK/AC000045
SI  - GENBANK/AC002059
SI  - GENBANK/AJ010228
SI  - GENBANK/AJ010229
SI  - GENBANK/AJ010230
SI  - GENBANK/AJ010231
SI  - GENBANK/AJ010232
SI  - GENBANK/AJ010233
SI  - GENBANK/AL008723
SI  - GENBANK/AL021937
SI  - GENBANK/AL022321
SI  - GENBANK/Z83839
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Genome Res
JT  - Genome research
JID - 9518021
RN  - 0 (AP1B1 protein, human)
RN  - 0 (Adaptor Protein Complex 1)
RN  - 0 (Adaptor Protein Complex beta Subunits)
RN  - 0 (Carrier Proteins)
RN  - 0 (DNA, Antisense)
RN  - 0 (Membrane Proteins)
RN  - 0 (RFPL1 protein, human)
RN  - 0 (RFPL2 protein, human)
RN  - 0 (RFPL3 protein, human)
SB  - IM
MH  - *Adaptor Protein Complex 1
MH  - Adaptor Protein Complex beta Subunits
MH  - Amino Acid Sequence
MH  - Base Sequence
MH  - Carrier Proteins/*genetics
MH  - *Chromosomes, Human, Pair 22
MH  - Contig Mapping
MH  - DNA, Antisense/genetics
MH  - Female
MH  - *Gene Duplication
MH  - Humans
MH  - Male
MH  - Membrane Proteins/genetics
MH  - Models, Genetic
MH  - Molecular Sequence Data
MH  - Multigene Family
MH  - Pedigree
MH  - Polymorphism, Genetic
MH  - Pseudogenes/genetics
MH  - Sequence Homology, Amino Acid
MH  - Syndrome
MH  - Tissue Distribution
MH  - Transcription, Genetic
EDAT- 1999/10/06 00:00
MHDA- 1999/10/06 00:01
CRDT- 1999/10/06 00:00
PHST- 1999/10/06 00:00 [pubmed]
PHST- 1999/10/06 00:01 [medline]
PHST- 1999/10/06 00:00 [entrez]
AID - 10.1101/gr.9.9.803 [doi]
PST - ppublish
SO  - Genome Res. 1999 Sep;9(9):803-14. doi: 10.1101/gr.9.9.803.