P47914 (RL29_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
60S ribosomal protein L29

Alternative name(s):
Cell surface heparin-binding protein HIP

Gene names

Name:

RPL29

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	159 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the ribosomal protein L29e family.

Ontologies

Keywords
Domain	Repeat
Ligand	Heparin-binding
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Acetylation Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	SRP-dependent cotranslational protein targeting to membrane Traceable author statement. Source: Reactome embryo implantation Traceable author statement Ref.3. Source: ProtInc nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Traceable author statement. Source: Reactome translational elongation Traceable author statement. Source: Reactome translational initiation Traceable author statement. Source: Reactome translational termination Traceable author statement. Source: Reactome viral transcription Traceable author statement. Source: Reactome
Cellular_component	cytosolic large ribosomal subunit Inferred from direct assay Ref.6. Source: UniProtKB
Molecular_function	RNA binding Traceable author statement Ref.2. Source: ProtInc heparin binding Traceable author statement Ref.3. Source: ProtInc structural constituent of ribosome Non-traceable author statement Ref.6. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DDX56	Q9NY93	1	EBI-714039,EBI-372376
PSTPIP1	O43586	1	EBI-714039,EBI-1050964

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.6
	Chain	2 – 159	158	60S ribosomal protein L29		PRO_0000219134
Amino acid modifications
	Modified residue	5	1	N6-methyllysine Ref.6
	Modified residue	33	1	N6-acetyllysine Ref.8
	Modified residue	142	1	Phosphoserine Ref.9
	Cross-link	56		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7
	Cross-link	73		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7
Experimental info
	Sequence conflict	5	1	K → R in BAF82227. Ref.4
	Sequence conflict	120	1	R → A in CAA89008. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P47914 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 2A0C31984EF4FF95	FASTA	159	17,752
	10 20 30 40 50 60 MAKSKNHTTH NQSRKWHRNG IKKPRSQRYE SLKGVDPKFL RNMRFAKKHN KKGLKKMQAN 70 80 90 100 110 120 NAKAMSARAE AIKALVKPKE VKPKIPKGVS RKLDRLAYIA HPKLGKRARA RIAKGLRLCR 130 140 150 PKAKAKAKAK DQTKAQAAAP ASVPAQAPKR TQAPTKASE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Law P.T., Tsui S.K., Lee C.Y., Waye M.M. Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"A novel cDNA encoding a human homologue of ribosomal protein L29." Law P.T., Tsui S.K.W., Lam W.Y., Luk S.C., Hwang D.M., Liew C.C., Lee C.-Y., Fung K.-P., Waye M.M.Y. Biochim. Biophys. Acta 1305:105-108(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"cDNA cloning and expression of HIP, a novel cell surface heparan sulfate/heparin-binding protein of human uterine epithelial cells and cell lines." Liu S., Smith S.E., Julian J., Rohde L.H., Karin N.J., Carson D.D. J. Biol. Chem. 271:11817-11823(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Cerebellum.
[5]	"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]. Tissue: Ovary and Pancreas.
[6]	"Characterization and analysis of posttranslational modifications of the human large cytoplasmic ribosomal subunit proteins by mass spectrometry and Edman sequencing." Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R., Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B., Karpova G.G. J. Protein Chem. 22:249-258(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-15, MASS SPECTROMETRY, METHYLATION AT LYS-5.
[7]	"Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry." Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D. Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-56 AND LYS-73, MASS SPECTROMETRY. Tissue: Mammary cancer.
[8]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33, MASS SPECTROMETRY.
[9]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U10248 mRNA. Translation: AAC50499.1. Z49148 mRNA. Translation: CAA89008.1. U49083 mRNA. Translation: AAC50647.1. AK289538 mRNA. Translation: BAF82227.1. AK311884 mRNA. Translation: BAG34825.1. BC008926 mRNA. Translation: AAH08926.1. BC070190 mRNA. Translation: AAH70190.1. BC070481 mRNA. Translation: AAH70481.1. BC071663 mRNA. Translation: AAH71663.1.
IPI	IPI00419919.
PIR	S65784.
RefSeq	NP_000983.1. NM_000992.2.
UniGene	Hs.425125.
3D structure databases
ProteinModelPortal	P47914.
ModBase	Search...
Protein-protein interaction databases
IntAct	P47914. 7 interactions.
MINT	MINT-1375294.
STRING	9606.ENSP00000294189.
PTM databases
PhosphoSite	P47914.
Polymorphism databases
DMDM	1350706.
Proteomic databases
PaxDb	P47914.
PRIDE	P47914.
Protocols and materials databases
DNASU	6159.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000294189; ENSP00000294189; ENSG00000162244. ENST00000466397; ENSP00000418868; ENSG00000162244. ENST00000475248; ENSP00000417048; ENSG00000162244. ENST00000479017; ENSP00000418153; ENSG00000162244. ENST00000492277; ENSP00000418346; ENSG00000162244. ENST00000495383; ENSP00000420673; ENSG00000162244.
GeneID	6159.
KEGG	hsa:6159.
UCSC	uc003dcs.3. human.
Organism-specific databases
CTD	6159.
GeneCards	GC03M052029.
H-InvDB	HIX0031209.
HGNC	HGNC:10331. RPL29.
MIM	601832. gene.
neXtProt	NX_P47914.
PharmGKB	PA34711.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG249125.
HOVERGEN	HBG000386.
InParanoid	P47914.
KO	K02905.
OMA	KGTQAPT.
OrthoDB	EOG49S67R.
PhylomeDB	P47914.
Enzyme and pathway databases
Reactome	REACT_116125. Disease. REACT_17015. Metabolism of proteins. REACT_1762. 3' -UTR-mediated translational regulation. REACT_21257. Metabolism of RNA. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	P47914.
Bgee	P47914.
CleanEx	HS_RPL29.
Genevestigator	P47914.
GermOnline	ENSG00000162244. Homo sapiens.
Family and domain databases
InterPro	IPR002673. Ribosomal_L29e. [Graphical view]
PANTHER	PTHR12884. PTHR12884. 1 hit.
Pfam	PF01779. Ribosomal_L29e. 1 hit. [Graphical view]
ProDom	PD010314. Ribosomal_L29e. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...
Other
ChiTaRS	RPL29. human.
GenomeRNAi	6159.
NextBio	23919.
SOURCE	Search...

Entry information

Entry name

RL29_HUMAN

Accession

Primary (citable) accession number: P47914
Secondary accession number(s): A8K0H3, B2R4M8, Q6IPY3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.