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P35268

- RL22_HUMAN

UniProt

P35268 - RL22_HUMAN

Protein

60S ribosomal protein L22

Gene

RPL22

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

    GO - Molecular functioni

    1. heparin binding Source: UniProtKB-KW
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: UniProt
    4. RNA binding Source: ProtInc
    5. structural constituent of ribosome Source: UniProtKB

    GO - Biological processi

    1. alpha-beta T cell differentiation Source: Ensembl
    2. cellular protein metabolic process Source: Reactome
    3. gene expression Source: Reactome
    4. mRNA metabolic process Source: Reactome
    5. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
    6. RNA metabolic process Source: Reactome
    7. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
    8. translation Source: UniProtKB
    9. translational elongation Source: Reactome
    10. translational initiation Source: Reactome
    11. translational termination Source: Reactome
    12. viral life cycle Source: Reactome
    13. viral process Source: Reactome
    14. viral transcription Source: Reactome

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Ligandi

    Heparin-binding, RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
    REACT_1404. Peptide chain elongation.
    REACT_1797. Formation of a pool of free 40S subunits.
    REACT_1986. Eukaryotic Translation Termination.
    REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
    REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
    REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
    REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
    REACT_9491. Viral mRNA Translation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    60S ribosomal protein L22
    Alternative name(s):
    EBER-associated protein
    Short name:
    EAP
    Epstein-Barr virus small RNA-associated protein
    Heparin-binding protein HBp15
    Gene namesi
    Name:RPL22
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:10315. RPL22.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. cytosol Source: Reactome
    3. cytosolic large ribosomal subunit Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProt
    5. nucleus Source: UniProt
    6. ribonucleoprotein complex Source: MGI

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34688.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 12812760S ribosomal protein L22PRO_0000215501Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei69 – 691N6-succinyllysineBy similarity

    Proteomic databases

    MaxQBiP35268.
    PaxDbiP35268.
    PeptideAtlasiP35268.
    PRIDEiP35268.

    2D gel databases

    SWISS-2DPAGEP35268.

    PTM databases

    PhosphoSiteiP35268.

    Expressioni

    Gene expression databases

    ArrayExpressiP35268.
    BgeeiP35268.
    CleanExiHS_RPL22.
    GenevestigatoriP35268.

    Interactioni

    Protein-protein interaction databases

    BioGridi112066. 91 interactions.
    IntActiP35268. 30 interactions.
    MINTiMINT-1149755.
    STRINGi9606.ENSP00000346088.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Belectron microscopy5.00U1-128[»]
    ProteinModelPortaliP35268.
    SMRiP35268. Positions 15-126.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi120 – 1289Asp/Glu-rich (highly acidic)

    Sequence similaritiesi

    Belongs to the ribosomal protein L22e family.Curated

    Phylogenomic databases

    eggNOGiNOG260326.
    HOGENOMiHOG000198396.
    HOVERGENiHBG004373.
    InParanoidiP35268.
    KOiK02891.
    OMAiCKQPAND.
    PhylomeDBiP35268.
    TreeFamiTF313018.

    Family and domain databases

    InterProiIPR002671. Ribosomal_L22e.
    [Graphical view]
    PANTHERiPTHR10064. PTHR10064. 1 hit.
    PfamiPF01776. Ribosomal_L22e. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P35268-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPVKKLVVK GGKKKKQVLK FTLDCTHPVE DGIMDAANFE QFLQERIKVN    50
    GKAGNLGGGV VTIERSKSKI TVTSEVPFSK RYLKYLTKKY LKKNNLRDWL 100
    RVVANSKESY ELRYFQINQD EEEEEDED 128
    Length:128
    Mass (Da):14,787
    Last modified:January 23, 2007 - v2
    Checksum:i0F3ED8BE70C9F962
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59357 mRNA. Translation: CAA42007.1.
    D17652 mRNA. Translation: BAA04545.1.
    AK311749 mRNA. Translation: BAG34692.1.
    CR456873 mRNA. Translation: CAG33154.1.
    AL031847 Genomic DNA. Translation: CAI19448.1.
    CH471130 Genomic DNA. Translation: EAW71518.1.
    BC035566 mRNA. Translation: AAH35566.1.
    BC058887 mRNA. Translation: AAH58887.1.
    BC066314 mRNA. Translation: AAH66314.1.
    CCDSiCCDS58.1.
    PIRiJC2120.
    RefSeqiNP_000974.1. NM_000983.3.
    UniGeneiHs.515329.
    Hs.554762.

    Genome annotation databases

    EnsembliENST00000234875; ENSP00000346088; ENSG00000116251.
    GeneIDi6146.
    KEGGihsa:6146.
    UCSCiuc001amd.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59357 mRNA. Translation: CAA42007.1 .
    D17652 mRNA. Translation: BAA04545.1 .
    AK311749 mRNA. Translation: BAG34692.1 .
    CR456873 mRNA. Translation: CAG33154.1 .
    AL031847 Genomic DNA. Translation: CAI19448.1 .
    CH471130 Genomic DNA. Translation: EAW71518.1 .
    BC035566 mRNA. Translation: AAH35566.1 .
    BC058887 mRNA. Translation: AAH58887.1 .
    BC066314 mRNA. Translation: AAH66314.1 .
    CCDSi CCDS58.1.
    PIRi JC2120.
    RefSeqi NP_000974.1. NM_000983.3.
    UniGenei Hs.515329.
    Hs.554762.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3J3B electron microscopy 5.00 U 1-128 [» ]
    ProteinModelPortali P35268.
    SMRi P35268. Positions 15-126.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112066. 91 interactions.
    IntActi P35268. 30 interactions.
    MINTi MINT-1149755.
    STRINGi 9606.ENSP00000346088.

    PTM databases

    PhosphoSitei P35268.

    2D gel databases

    SWISS-2DPAGE P35268.

    Proteomic databases

    MaxQBi P35268.
    PaxDbi P35268.
    PeptideAtlasi P35268.
    PRIDEi P35268.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000234875 ; ENSP00000346088 ; ENSG00000116251 .
    GeneIDi 6146.
    KEGGi hsa:6146.
    UCSCi uc001amd.3. human.

    Organism-specific databases

    CTDi 6146.
    GeneCardsi GC01M006179.
    HGNCi HGNC:10315. RPL22.
    MIMi 180474. gene.
    neXtProti NX_P35268.
    PharmGKBi PA34688.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG260326.
    HOGENOMi HOG000198396.
    HOVERGENi HBG004373.
    InParanoidi P35268.
    KOi K02891.
    OMAi CKQPAND.
    PhylomeDBi P35268.
    TreeFami TF313018.

    Enzyme and pathway databases

    Reactomei REACT_115902. SRP-dependent cotranslational protein targeting to membrane.
    REACT_1404. Peptide chain elongation.
    REACT_1797. Formation of a pool of free 40S subunits.
    REACT_1986. Eukaryotic Translation Termination.
    REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
    REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
    REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
    REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
    REACT_9491. Viral mRNA Translation.

    Miscellaneous databases

    GeneWikii RPL22.
    GenomeRNAii 6146.
    NextBioi 23879.
    PROi P35268.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35268.
    Bgeei P35268.
    CleanExi HS_RPL22.
    Genevestigatori P35268.

    Family and domain databases

    InterProi IPR002671. Ribosomal_L22e.
    [Graphical view ]
    PANTHERi PTHR10064. PTHR10064. 1 hit.
    Pfami PF01776. Ribosomal_L22e. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "EAP, a highly conserved cellular protein associated with Epstein-Barr virus small RNAs (EBERs)."
      Toczyski D.P.W., Steitz J.A.
      EMBO J. 10:459-466(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-46 AND 108-125.
      Tissue: Placenta.
    2. "A novel heparin-binding protein, HBp15, is identified as mammalian ribosomal protein L22."
      Fujita Y., Okamoto T., Noshiro M., Kato Y., Takada K., Sato J.D., Ozaki T., McKeehan W.L., Crabb J.W., Whitney R.G.
      Biochem. Biophys. Res. Commun. 199:706-713(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Submandibular gland.
    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].
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. Bienvenut W.V., Calvo F., Kolch W.
      Submitted (FEB-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-10; 53-65; 70-81 AND 102-113, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma.
    6. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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: Brain, Cervix and Eye.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

    Entry informationi

    Entry nameiRL22_HUMAN
    AccessioniPrimary (citable) accession number: P35268
    Secondary accession number(s): B2R495, Q6IBD1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 136 of the entry and version 2 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

    Miscellaneous

    Binds to Epstein-Barr virus small RNAs and to heparin.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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