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Protein

39S ribosomal protein L11, mitochondrial

Gene

MRPL11

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • structural constituent of ribosome Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_267634. Mitochondrial translation initiation.
REACT_268133. Mitochondrial translation elongation.
REACT_268261. Mitochondrial translation termination.

Names & Taxonomyi

Protein namesi
Recommended name:
39S ribosomal protein L11, mitochondrial
Short name:
L11mt
Short name:
MRP-L11
Gene namesi
Name:MRPL11
ORF Names:CGI-113
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:14042. MRPL11.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: Reactome
  • mitochondrial ribosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30940.

Polymorphism and mutation databases

BioMutaiMRPL11.
DMDMi22001931.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 19239S ribosomal protein L11, mitochondrialPRO_0000030443
Transit peptidei1 – ?MitochondrionSequence Analysis

Proteomic databases

MaxQBiQ9Y3B7.
PaxDbiQ9Y3B7.
PRIDEiQ9Y3B7.

PTM databases

PhosphoSiteiQ9Y3B7.

Expressioni

Gene expression databases

BgeeiQ9Y3B7.
CleanExiHS_MRPL11.
ExpressionAtlasiQ9Y3B7. baseline and differential.
GenevisibleiQ9Y3B7. HS.

Organism-specific databases

HPAiHPA057685.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CAMK2BQ135543EBI-5453723,EBI-1058722
CAMK2DQ135573EBI-5453723,EBI-351018
FSD2A1L4K13EBI-5453723,EBI-5661036
gagP045913EBI-5453723,EBI-6179727From a different organism.
HEL-S-101V9HW273EBI-5453723,EBI-10178933
HMBOX1Q6NT763EBI-5453723,EBI-2549423
HOMEZQ8IX15-33EBI-5453723,EBI-10172004
JAKMIP2Q96AA83EBI-5453723,EBI-752007
KRT40Q6A1623EBI-5453723,EBI-10171697
PNMA1Q8ND903EBI-5453723,EBI-302345
SLC16A9Q7RTY13EBI-5453723,EBI-10232636
TAX1BP1Q86VP13EBI-5453723,EBI-529518
TFCP2Q128003EBI-5453723,EBI-717422
THAP1Q9NVV93EBI-5453723,EBI-741515
VPS52Q8N1B43EBI-5453723,EBI-2799833

Protein-protein interaction databases

BioGridi122369. 56 interactions.
IntActiQ9Y3B7. 16 interactions.
MINTiMINT-3085719.
STRINGi9606.ENSP00000308897.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J7Yelectron microscopy3.40J1-192[»]
3J9Melectron microscopy3.50J1-192[»]
ProteinModelPortaliQ9Y3B7.
SMRiQ9Y3B7. Positions 18-157.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L11P family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0080.
GeneTreeiENSGT00390000003153.
HOGENOMiHOG000082123.
HOVERGENiHBG036110.
InParanoidiQ9Y3B7.
KOiK02867.
OMAiCKDFNER.
OrthoDBiEOG7HHWTP.
PhylomeDBiQ9Y3B7.
TreeFamiTF313471.

Family and domain databases

Gene3Di1.10.10.250. 1 hit.
3.30.1550.10. 1 hit.
HAMAPiMF_00736. Ribosomal_L11.
InterProiIPR000911. Ribosomal_L11/L12.
IPR006519. Ribosomal_L11_bac-typ.
IPR020783. Ribosomal_L11_C.
IPR020784. Ribosomal_L11_N.
[Graphical view]
PANTHERiPTHR11661. PTHR11661. 1 hit.
PfamiPF00298. Ribosomal_L11. 1 hit.
PF03946. Ribosomal_L11_N. 1 hit.
[Graphical view]
SMARTiSM00649. RL11. 1 hit.
[Graphical view]
SUPFAMiSSF46906. SSF46906. 1 hit.
SSF54747. SSF54747. 1 hit.
TIGRFAMsiTIGR01632. L11_bact. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y3B7-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSKLGRAARG LRKPEVGGVI RAIVRAGLAM PGPPLGPVLG QRGVSINQFC
60 70 80 90 100
KEFNERTKDI KEGIPLPTKI LVKPDRTFEI KIGQPTVSYF LKAAAGIEKG
110 120 130 140 150
ARQTGKEVAG LVTLKHVYEI ARIKAQDEAF ALQDVPLSSV VRSIIGSARS
160 170 180 190
LGIRVVKDLS SEELAAFQKE RAIFLAAQKE ADLAAQEEAA KK
Length:192
Mass (Da):20,683
Last modified:November 1, 1999 - v1
Checksum:i92506A20044BF278
GO
Isoform 2 (identifier: Q9Y3B7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     16-41: Missing.

Show »
Length:166
Mass (Da):18,205
Checksum:iA78DA10D323B1D24
GO
Isoform 3 (identifier: Q9Y3B7-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     158-192: DLSSEELAAFQKERAIFLAAQKEADLAAQEEAAKK → ERCSANVLRNGKISMKDPSGRSSV

Note: No experimental confirmation available.Curated
Show »
Length:181
Mass (Da):19,454
Checksum:i578392577167303F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681T → I in BM554886 (PubMed:15489334).Curated
Isoform 3 (identifier: Q9Y3B7-3)
Sequence conflicti181 – 1811V → L in BM554886 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei16 – 4126Missing in isoform 2. 1 PublicationVSP_041077Add
BLAST
Alternative sequencei158 – 19235DLSSE…EAAKK → ERCSANVLRNGKISMKDPSG RSSV in isoform 3. 1 PublicationVSP_045237Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB049638 mRNA. Translation: BAB40843.1.
AF151871 mRNA. Translation: AAD34108.1.
AK290084 mRNA. Translation: BAF82773.1.
AP002748 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74528.1.
CH471076 Genomic DNA. Translation: EAW74529.1.
CH471076 Genomic DNA. Translation: EAW74531.1.
BC005002 mRNA. Translation: AAH05002.1.
BC108277 mRNA. Translation: AAI08278.1.
BM554886 mRNA. No translation available.
AB051338 Genomic DNA. Translation: BAB54928.1.
CCDSiCCDS44655.1. [Q9Y3B7-2]
CCDS8139.1. [Q9Y3B7-1]
CCDS8140.1. [Q9Y3B7-3]
RefSeqiNP_057134.1. NM_016050.4. [Q9Y3B7-1]
NP_733934.1. NM_170738.3. [Q9Y3B7-2]
NP_733935.1. NM_170739.3. [Q9Y3B7-3]
UniGeneiHs.418450.

Genome annotation databases

EnsembliENST00000310999; ENSP00000308897; ENSG00000174547. [Q9Y3B7-1]
ENST00000329819; ENSP00000329630; ENSG00000174547. [Q9Y3B7-3]
ENST00000430466; ENSP00000415356; ENSG00000174547. [Q9Y3B7-2]
GeneIDi65003.
KEGGihsa:65003.
UCSCiuc001ohy.4. human.
uc001ohz.4. human. [Q9Y3B7-1]
uc001oia.4. human. [Q9Y3B7-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB049638 mRNA. Translation: BAB40843.1.
AF151871 mRNA. Translation: AAD34108.1.
AK290084 mRNA. Translation: BAF82773.1.
AP002748 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74528.1.
CH471076 Genomic DNA. Translation: EAW74529.1.
CH471076 Genomic DNA. Translation: EAW74531.1.
BC005002 mRNA. Translation: AAH05002.1.
BC108277 mRNA. Translation: AAI08278.1.
BM554886 mRNA. No translation available.
AB051338 Genomic DNA. Translation: BAB54928.1.
CCDSiCCDS44655.1. [Q9Y3B7-2]
CCDS8139.1. [Q9Y3B7-1]
CCDS8140.1. [Q9Y3B7-3]
RefSeqiNP_057134.1. NM_016050.4. [Q9Y3B7-1]
NP_733934.1. NM_170738.3. [Q9Y3B7-2]
NP_733935.1. NM_170739.3. [Q9Y3B7-3]
UniGeneiHs.418450.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J7Yelectron microscopy3.40J1-192[»]
3J9Melectron microscopy3.50J1-192[»]
ProteinModelPortaliQ9Y3B7.
SMRiQ9Y3B7. Positions 18-157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122369. 56 interactions.
IntActiQ9Y3B7. 16 interactions.
MINTiMINT-3085719.
STRINGi9606.ENSP00000308897.

PTM databases

PhosphoSiteiQ9Y3B7.

Polymorphism and mutation databases

BioMutaiMRPL11.
DMDMi22001931.

Proteomic databases

MaxQBiQ9Y3B7.
PaxDbiQ9Y3B7.
PRIDEiQ9Y3B7.

Protocols and materials databases

DNASUi65003.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000310999; ENSP00000308897; ENSG00000174547. [Q9Y3B7-1]
ENST00000329819; ENSP00000329630; ENSG00000174547. [Q9Y3B7-3]
ENST00000430466; ENSP00000415356; ENSG00000174547. [Q9Y3B7-2]
GeneIDi65003.
KEGGihsa:65003.
UCSCiuc001ohy.4. human.
uc001ohz.4. human. [Q9Y3B7-1]
uc001oia.4. human. [Q9Y3B7-2]

Organism-specific databases

CTDi65003.
GeneCardsiGC11M066202.
HGNCiHGNC:14042. MRPL11.
HPAiHPA057685.
MIMi611826. gene.
neXtProtiNX_Q9Y3B7.
PharmGKBiPA30940.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0080.
GeneTreeiENSGT00390000003153.
HOGENOMiHOG000082123.
HOVERGENiHBG036110.
InParanoidiQ9Y3B7.
KOiK02867.
OMAiCKDFNER.
OrthoDBiEOG7HHWTP.
PhylomeDBiQ9Y3B7.
TreeFamiTF313471.

Enzyme and pathway databases

ReactomeiREACT_267634. Mitochondrial translation initiation.
REACT_268133. Mitochondrial translation elongation.
REACT_268261. Mitochondrial translation termination.

Miscellaneous databases

ChiTaRSiMRPL11. human.
GeneWikiiMRPL11.
GenomeRNAii65003.
NextBioi67180.
PROiQ9Y3B7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y3B7.
CleanExiHS_MRPL11.
ExpressionAtlasiQ9Y3B7. baseline and differential.
GenevisibleiQ9Y3B7. HS.

Family and domain databases

Gene3Di1.10.10.250. 1 hit.
3.30.1550.10. 1 hit.
HAMAPiMF_00736. Ribosomal_L11.
InterProiIPR000911. Ribosomal_L11/L12.
IPR006519. Ribosomal_L11_bac-typ.
IPR020783. Ribosomal_L11_C.
IPR020784. Ribosomal_L11_N.
[Graphical view]
PANTHERiPTHR11661. PTHR11661. 1 hit.
PfamiPF00298. Ribosomal_L11. 1 hit.
PF03946. Ribosomal_L11_N. 1 hit.
[Graphical view]
SMARTiSM00649. RL11. 1 hit.
[Graphical view]
SUPFAMiSSF46906. SSF46906. 1 hit.
SSF54747. SSF54747. 1 hit.
TIGRFAMsiTIGR01632. L11_bact. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structural compensation for the deficit of rRNA with proteins in the mammalian mitochondrial ribosome. Systematic analysis of protein components of the large ribosomal subunit from mammalian mitochondria."
    Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A., Watanabe K.
    J. Biol. Chem. 276:21724-21736(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
  2. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
    Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
    Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "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] (ISOFORM 1).
    Tissue: Subthalamic nucleus.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS 1; 2 AND 3).
    Tissue: Duodenum, Lymph and Melanoma.
  7. "The human mitochondrial ribosomal protein genes: mapping of 54 genes to the chromosomes and implications for human disorders."
    Kenmochi N., Suzuki T., Uechi T., Magoori M., Kuniba M., Higa S., Watanabe K., Tanaka T.
    Genomics 77:65-70(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-141 (ISOFORMS 1/2).
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRM11_HUMAN
AccessioniPrimary (citable) accession number: Q9Y3B7
Secondary accession number(s): A6NLT0
, A8K219, Q32P46, Q96Q73
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: November 1, 1999
Last modified: June 24, 2015
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Ribosomal proteins
    Ribosomal proteins families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.