P62913 (RL11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
60S ribosomal protein L11

Alternative name(s):
CLL-associated antigen KW-12

Gene names

Name:

RPL11

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	178 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)

Function	Binds to 5S ribosomal RNA By similarity. Required for rRNA maturation and formation of the 60S ribosomal subunits. Promotes nucleolar location of PML By similarity. Ref.9
Subunit structure	Interacts with PML and MDM2 By similarity.
Subcellular location	Nucleus › nucleolus By similarity.
Involvement in disease	Diamond-Blackfan anemia 7 (DBA7) [MIM:612562]: A form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of malignancy. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.13
Sequence similarities	Belongs to the ribosomal protein L5P family.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Disease	Diamond-Blackfan anemia Disease mutation
Ligand	RNA-binding rRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Acetylation Phosphoprotein
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 nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Traceable author statement. Source: Reactome protein localization to nucleus Inferred from sequence or structural similarity. Source: UniProtKB rRNA processing Inferred from mutant phenotype PubMed 18697920. Source: UniProtKB ribosomal large subunit biogenesis Inferred from mutant phenotype PubMed 18697920. Source: UniProtKB 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.8. Source: UniProtKB nucleolus Inferred from direct assay PubMed 15195100. Source: UniProtKB
Molecular_function	RNA binding Traceable author statement Ref.1. Source: ProtInc rRNA binding Inferred from electronic annotation. Source: UniProtKB-KW structural constituent of ribosome Non-traceable author statement Ref.8. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MDM2	Q00987	6	EBI-354380,EBI-389668

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P62913-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P62913-2)

The sequence of this isoform differs from the canonical sequence as follows:
     3-3: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.5
	Chain	2 – 178	177	60S ribosomal protein L11		PRO_0000125082
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.5 Ref.8
	Modified residue	44	1	Phosphothreonine Ref.10
	Modified residue	52	1	N6-acetyllysine Ref.11
	Modified residue	85	1	N6-acetyllysine Ref.11
Natural variations
	Alternative sequence	3	1	Missing in isoform 2.		VSP_008320
	Natural variant	20	1	L → H in DBA7. Ref.13		VAR_055448
	Natural variant	161	1	Missing in DBA7. Ref.9		VAR_055449
Experimental info
	Sequence conflict	31	1	D → G in CAA55816. Ref.1
	Sequence conflict	73	1	T → A in CAA55816. Ref.1
	Sequence conflict	92	1	Y → L in CAA55816. Ref.1
	Sequence conflict	118	1	K → E in CAA55816. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 26EC965C9239774E	FASTA	178	20,252
	10 20 30 40 50 60 MAQDQGEKEN PMRELRIRKL CLNICVGESG DRLTRAAKVL EQLTGQTPVF SKARYTVRSF 70 80 90 100 110 120 GIRRNEKIAV HCTVRGAKAE EILEKGLKVR EYELRKNNFS DTGNFGFGIQ EHIDLGIKYD 130 140 150 160 170 PSIGIYGLDF YVVLGRPGFS IADKKRRTGC IGAKHRISKE EAMRWFQQKY DGIILPGK
	Isoform 2 [UniParc] [UniParc]. Checksum: 534FC28B1D3CF195	FASTA	177	20,124
	10 20 30 40 50 60 MADQGEKENP MRELRIRKLC LNICVGESGD RLTRAAKVLE QLTGQTPVFS KARYTVRSFG 70 80 90 100 110 120 IRRNEKIAVH CTVRGAKAEE ILEKGLKVRE YELRKNNFSD TGNFGFGIQE HIDLGIKYDP 130 140 150 160 170 SIGIYGLDFY VVLGRPGFSI ADKKRRTGCI GAKHRISKEE AMRWFQQKYD GIILPGK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and determination of the primary structure of DNA complementary to the mRNA of human ribosomal protein L11." Mishin V.P., Filipenko M.L., Muravlev A.I., Karpova G.G., Mertvetsov N.P. Bioorg. Khim. 21:158-160(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Expressed sequence tags from a human cell line." Bhat K.S. Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Structural and functional analysis of the human ribosomal protein L11 gene." Voronina E.N., Kolokol'tsova T.D., Nechaeva E.A., Filipenko M.L. Mol. Biol. (Mosk.) 37:425-435(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"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] (ISOFORM 2). Tissue: Tonsil.
[5]	Quadroni M., Bienvenut W.V. Submitted (NOV-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-13; 89-95; 119-145 AND 157-164, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"Identification of novel tumor antigens in CLL by SEREX: assessment of their potential as targets for immunotherapeutic approaches." Krackhardt A.M., Witzens M., Harig S., Hodi F.S., Zauls A.J., Chessia M., Barrett P., Gribben J.G. Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-178 (ISOFORM 1).
[7]	"A map of 75 human ribosomal protein genes." Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J., Tanaka T., Page D.C. Genome Res. 8:509-523(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-52.
[8]	"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: MASS SPECTROMETRY, ACETYLATION AT ALA-2.
[9]	"Ribosomal protein L5 and L11 mutations are associated with cleft palate and abnormal thumbs in Diamond-Blackfan anemia patients." Gazda H.T., Sheen M.R., Vlachos A., Choesmel V., O'Donohue M.-F., Schneider H., Darras N., Hasman C., Sieff C.A., Newburger P.E., Ball S.E., Niewiadomska E., Matysiak M., Zaucha J.M., Glader B., Niemeyer C., Meerpohl J.J., Atsidaftos E. , Lipton J.M., Gleizes P.-E., Beggs A.H. Am. J. Hum. Genet. 83:769-780(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, VARIANT DBA7 GLU-161 DEL.
[10]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-44, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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-52 AND LYS-85, MASS SPECTROMETRY.
[12]	"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].
[13]	"Identification of mutations in the ribosomal protein L5 (RPL5) and ribosomal protein L11 (RPL11) genes in Czech patients with Diamond-Blackfan anemia." Cmejla R., Cmejlova J., Handrkova H., Petrak J., Petrtylova K., Mihal V., Stary J., Cerna Z., Jabali Y., Pospisilova D. Hum. Mutat. 30:321-327(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT DBA7 HIS-20.
+	Additional computationally mapped references.

Web resources

Diamond-Blackfan Anemia mutation database

Cross-references

Sequence databases
EMBL GenBank DDBJ	X79234 mRNA. Translation: CAA55816.1. L05092 mRNA. Translation: AAC15856.1. AF101385 Genomic DNA. Translation: AAD20460.3. BC018970 mRNA. Translation: AAH18970.1. AF432212 mRNA. Translation: AAL99919.1. AB007171 Genomic DNA. Translation: BAA25831.1.
IPI	IPI00376798. IPI00746438.
PIR	S45049.
RefSeq	NP_000966.2. NM_000975.3. NP_001186731.1. NM_001199802.1.
UniGene	Hs.719951.
3D structure databases
ProteinModelPortal	P62913.
ModBase	Search...
Protein-protein interaction databases
IntAct	P62913. 23 interactions.
MINT	MINT-1140097.
STRING	9606.ENSP00000363676.
PTM databases
PhosphoSite	P62913.
Polymorphism databases
DMDM	51702795.
2D gel databases
SWISS-2DPAGE	P62913.
Proteomic databases
PaxDb	P62913.
PRIDE	P62913.
Protocols and materials databases
DNASU	6135.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000374550; ENSP00000363676; ENSG00000142676.
GeneID	6135.
KEGG	hsa:6135.
UCSC	uc001bhk.3. human. uc001bhl.3. human.
Organism-specific databases
CTD	6135.
GeneCards	GC01P024018.
HGNC	HGNC:10301. RPL11.
HPA	HPA002734.
MIM	604175. gene. 612562. phenotype.
neXtProt	NX_P62913.
Orphanet	124. Blackfan-Diamond disease.
PharmGKB	PA34664.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0094.
HOGENOM	HOG000231312.
HOVERGEN	HBG055214.
InParanoid	P62913.
KO	K02868.
OMA	HMGVGES.
OrthoDB	EOG4BG8X4.
PhylomeDB	P62913.
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	P62913.
Bgee	P62913.
CleanEx	HS_RPL11.
Genevestigator	P62913.
GermOnline	ENSG00000142676. Homo sapiens.
Family and domain databases
Gene3D	3.30.1440.10. 1 hit.
InterPro	IPR002132. Ribosomal_L5. IPR020929. Ribosomal_L5_CS. IPR022803. Ribosomal_L5_domain. [Graphical view]
PANTHER	PTHR11994. PTHR11994. 1 hit.
Pfam	PF00281. Ribosomal_L5. 1 hit. PF00673. Ribosomal_L5_C. 1 hit. [Graphical view]
PIRSF	PIRSF002161. Ribosomal_L5. 1 hit.
SUPFAM	SSF55282. Ribosomal_L5. 1 hit.
PROSITE	PS00358. RIBOSOMAL_L5. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	RPL11. human.
GenomeRNAi	6135.
NextBio	23831.
PMAP-CutDB	P62913.
SOURCE	Search...

Entry information

Entry name

RL11_HUMAN

Accession

Primary (citable) accession number: P62913
Secondary accession number(s): P25121 , P39026, Q8TDH2, Q9Y674

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 93 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.