Identification, expression pattern, and subcellular location of human RIP isoforms.
XRIP alpha was identified as an adapter protein involved in RAP nuclear import. Several homologs were reported in mammal EST analysis, but the expression pattern and genomic organization of hRIP isoforms were not clarified yet. We isolated nine isoforms of hRIP from a premade human fetal brain library. hRIP alpha is the longest isoform with 219 residues, containing a N-terminal arginine-rich basic region, followed by an acidic region and two C-terminal Zn finger-like structures. hRIP beta deletes one Zn-finger-like structure. Three hRIP alpha isoforms and four hRIP sigma isoforms express truncated proteins due to frame shift. hRIP gamma isoforms lost the C-terminal Zn-finger-like structure. hRIP delta isoforms only contain the N-terminal arginine-rich basic region and the core sequence of the acidic region. The genomic organization of hRIP was identified by bioinformatic analysis. hRIP, containing seven exons, is located at human chromosome 17p13. hRIP was expressed in all 16 detected human tissues with a similar pattern. All EGFP-hRIP fusion proteins were located at the nucleus in the HEK293 cell. The two-polar molecular structure of hRIP might be involved in the basic cell function, and plays a role in the alternative nuclear ingress.
Chen
Jin-Zhong
JZ
State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University, Shanghai, People's Republic of China.
Huang
Sheng-Dong
SD
Ji
Chao-Neng
CN
Pang
Rong-Yan
RY
Xie
Yi
Y
Xue
Jing-Lun
JL
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D001483:Base Sequence; D001921:Brain / Q000196:embryology / Q000378:metabolism; D002460:Cell Line; D002467:Cell Nucleus / Q000378:metabolism*; D002886:Chromosomes, Human, Pair 17; D019295:Computational Biology; D018076:DNA, Complementary; D019143:Evolution, Molecular; D005091:Exons; D016368:Frameshift Mutation; D015870:Gene Expression; D015894:Genome, Human; D049452:Green Fluorescent Proteins / Q000378:metabolism; D006801:Humans; D007438:Introns; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D020033:Protein Isoforms / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D011506:Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D053422:Receptor-Interacting Protein Serine-Threonine Kinases; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship; D014018:Tissue Distribution
D018076:DNA, Complementary; D020033:Protein Isoforms; D011506:Proteins; D011993:Recombinant Fusion Proteins; D049452:Green Fluorescent Proteins; C506249:RIPK1 protein, human; D053422:Receptor-Interacting Protein Serine-Threonine Kinases