60S ribosomal protein L29

60S ribosomal protein L29 is a protein that in humans is encoded by the RPL29 gene.[3][4]

RPL29
Available structures PDB Human UniProt search: PDBe RCSB List of PDB id codes 4UG0, 4V6X, 5AJ0, 4UJD, 4D67, 4D5Y, 4UJE, 4UJC
Identifiers
Aliases	RPL29, HIP, HUML29, RPL29P10, RPL29_3_370, ribosomal protein L29
External IDs	OMIM: 601832 HomoloGene: 133570 GeneCards: RPL29
Gene location (Human) Chr. Chromosome 3 (human)[1] Band 3p21.2 Start 51,993,522 bp[1] End 51,995,895 bp[1]
RNA expression pattern More reference expression data
Gene ontology Molecular function • heparin binding • RNA binding • structural constituent of ribosome • cadherin binding Cellular component • intracellular • cytosol • membrane • cytosolic large ribosomal subunit • ribosome Biological process • translational initiation • SRP-dependent cotranslational protein targeting to membrane • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay • cytoplasmic translation • embryo implantation • protein biosynthesis • viral transcription • rRNA processing Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	6159	n/a
Ensembl	ENSG00000162244	n/a
UniProt	P47914	n/a
RefSeq (mRNA)	NM_000992	n/a
RefSeq (protein)	NP_000983	n/a
Location (UCSC)	Chr 3: 51.99 – 52 Mb	n/a
PubMed search	[2]	n/a
Wikidata
View/Edit Human

Function

Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a cytoplasmic ribosomal protein that is a component of the 60S subunit. The protein belongs to the L29E family of ribosomal proteins. The protein is also a peripheral membrane protein expressed on the cell surface that directly binds heparin. Although this gene was previously reported to map to 3q29-qter, it is believed that it is located at 3p21.3-p21.2. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.[4]

Interactions

RPL29 has been shown to interact with BLMH.[5]

References

1. GRCh38: Ensembl release 89: ENSG00000162244 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. Law PT, Tsui SK, Lam WY, Luk SC, Hwang DM, Liew CC, Lee CY, Fung KP, Waye MM (Apr 1996). "A novel cDNA encoding a human homologue of ribosomal protein L29". Biochim Biophys Acta. 1305 (3): 105–8. doi:10.1016/0167-4781(95)00224-3. PMID 8597591.
4. "Entrez Gene: RPL29 ribosomal protein L29".
5. Koldamova RP, Lefterov IM, DiSabella MT, Almonte C, Watkins SC, Lazo JS (Jun 1999). "Human bleomycin hydrolase binds ribosomal proteins". Biochemistry. 38 (22): 7111–7. doi:10.1021/bi990135l. PMID 10353821.

Further reading

• Wool IG, Chan YL, Glück A (1996). "Structure and evolution of mammalian ribosomal proteins". Biochem. Cell Biol. 73 (11–12): 933–47. doi:10.1139/o95-101. PMID 8722009.
• Nika H, Hultin T (1984). "Location of the sulfhydryl groups involved in disulfide interaction between the neighboring proteins L6 and L29 in mammalian ribosomes. S-cleavage of the cyanylated proteins in polyacrylamide gels after separation by dodecylsulfate gel electrophoresis". Eur. J. Biochem. 142 (3): 521–6. doi:10.1111/j.1432-1033.1984.tb08316.x. PMID 6468376.
• Liu S, Smith SE, Julian J, Rohde LH, Karin NJ, Carson DD (1996). "cDNA cloning and expression of HIP, a novel cell surface heparan sulfate/heparin-binding protein of human uterine epithelial cells and cell lines". J. Biol. Chem. 271 (20): 11817–23. doi:10.1074/jbc.271.20.11817. PMID 8662616.
• Rohde LH, Julian J, Babaknia A, Carson DD (1996). "Cell surface expression of HIP, a novel heparin/heparan sulfate binding protein, of human uterine epithelial cells and cell lines". J. Biol. Chem. 271 (20): 11824–30. doi:10.1074/jbc.271.20.11824. PMID 8662617.
• Jacobs AL, Julian J, Sahin AA, Carson DD (1997). "Heparin/heparan sulfate interacting protein expression and functions in human breast cancer cells and normal breast epithelia". Cancer Res. 57 (22): 5148–54. PMID 9371517.
• Garcia-Barcelo M, Law PT, Tsui SK, Fung KP, Lee CY, Waye MM (1998). "Mapping of the human ribosomal large subunit protein gene RPL29 to human chromosome 3q29-qter". Genomics. 46 (1): 148–51. doi:10.1006/geno.1997.4990. PMID 9403071.
• Koldamova RP, Lefterov IM, DiSabella MT, Almonte C, Watkins SC, Lazo JS (1999). "Human bleomycin hydrolase binds ribosomal proteins". Biochemistry. 38 (22): 7111–7. doi:10.1021/bi990135l. PMID 10353821.
• Kudo H, Senju S, Mitsuya H, Nishimura Y (2000). "Mouse and human GTPBP2, newly identified members of the GP-1 family of GTPase". Biochem. Biophys. Res. Commun. 272 (2): 456–65. doi:10.1006/bbrc.2000.2763. PMID 10833435.
• Uechi T, Tanaka T, Kenmochi N (2001). "A complete map of the human ribosomal protein genes: assignment of 80 genes to the cytogenetic map and implications for human disorders". Genomics. 72 (3): 223–30. doi:10.1006/geno.2000.6470. PMID 11401437.
• Kirn-Safran CB, Julian J, Fongemie JE, Hoke DE, Czymmek KJ, Carson DD (2002). "Changes in the cytologic distribution of heparin/heparan sulfate interacting protein/ribosomal protein L29 (HIP/RPL29) during in vivo and in vitro mouse mammary epithelial cell expression and differentiation". Dev. Dyn. 223 (1): 70–84. doi:10.1002/dvdy.1226. PMID 11803571.
• Hoke DE, Carson DD, Höök M (2006). "A heparin binding synthetic peptide from human HIP / RPL29 fails to specifically differentiate between anticoagulantly active and inactive species of heparin". Journal of Negative Results in Biomedicine. 2: 1. doi:10.1186/1477-5751-2-1. PMC 152653. PMID 12659638.
• Odintsova TI, Müller EC, Ivanov AV, Egorov TA, Bienert R, Vladimirov SN, Kostka S, Otto A, Wittmann-Liebold B, Karpova GG (2004). "Characterization and analysis of posttranslational modifications of the human large cytoplasmic ribosomal subunit proteins by mass spectrometry and Edman sequencing". J. Protein Chem. 22 (3): 249–58. doi:10.1023/A:1025068419698. PMID 12962325.
• Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID 15635413.
• Nakanishi K, Komatsu Y, Kogawa N, Matsushita H (2005). "Analysis of eluted peptides from type 1 diabetes-susceptible HLA class II molecules identified novel islet protein, heparin/heparan sulfate-interacting protein". Biochem. Biophys. Res. Commun. 329 (1): 356–61. doi:10.1016/j.bbrc.2005.01.144. PMID 15721314.
• Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070.
• Liu JJ, Huang BH, Zhang J, Carson DD, Hooi SC (2006). "Repression of HIP/RPL29 expression induces differentiation in colon cancer cells". J. Cell. Physiol. 207 (2): 287–92. doi:10.1002/jcp.20589. PMID 16475173.

External links

• Overview of all the structural information available in the PDB for UniProt: P47914 (60S ribosomal protein L29) at the PDBe-KB.