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P15880

- RS2_HUMAN

UniProt

P15880 - RS2_HUMAN

Protein

40S ribosomal protein S2

Gene

RPS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. enzyme binding Source: UniProtKB
    2. fibroblast growth factor binding Source: UniProtKB
    3. mRNA binding Source: UniProtKB
    4. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. structural constituent of ribosome Source: UniProtKB

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. gene expression Source: Reactome
    3. mRNA metabolic process Source: Reactome
    4. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
    5. positive regulation of transferase activity Source: UniProtKB
    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

    Enzyme and pathway databases

    ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
    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_1979. Translation initiation complex formation.
    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_931. Ribosomal scanning and start codon recognition.
    REACT_9491. Viral mRNA Translation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    40S ribosomal protein S2
    Alternative name(s):
    40S ribosomal protein S4
    Protein LLRep3
    Gene namesi
    Name:RPS2
    Synonyms:RPS4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:10404. RPS2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. cytosolic small ribosomal subunit Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. membrane Source: UniProtKB
    5. nucleoplasm Source: UniProtKB
    6. nucleus Source: UniProt

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34806.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 29329240S ribosomal protein S2PRO_0000131673Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei263 – 2631N6-acetyllysine1 Publication
    Modified residuei264 – 2641Phosphoserine2 Publications
    Modified residuei275 – 2751N6-acetyllysine1 Publication
    Modified residuei281 – 2811Phosphoserine1 Publication

    Post-translational modificationi

    Citrullinated by PADI4 in the Arg/Gly-rich region.1 Publication
    Asymmetric arginine dimethylation by PRMT3 occurs at multiple sites in the Arg/Gly-rich region.

    Keywords - PTMi

    Acetylation, Citrullination, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP15880.
    PaxDbiP15880.
    PRIDEiP15880.

    PTM databases

    PhosphoSiteiP15880.

    Expressioni

    Gene expression databases

    BgeeiP15880.
    CleanExiHS_RPS2.
    GenevestigatoriP15880.

    Organism-specific databases

    HPAiHPA055133.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LRRK2Q5S0072EBI-443446,EBI-5323863

    Protein-protein interaction databases

    BioGridi112101. 169 interactions.
    IntActiP15880. 32 interactions.
    MINTiMINT-3008399.
    STRINGi9606.ENSP00000341885.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Aelectron microscopy5.00C1-293[»]
    ProteinModelPortaliP15880.
    SMRiP15880. Positions 53-278.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini102 – 16564S5 DRBMPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi22 – 5332Arg/Gly-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ribosomal protein S5P family.Curated
    Contains 1 S5 DRBM domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0098.
    HOGENOMiHOG000072596.
    HOVERGENiHBG000437.
    InParanoidiP15880.
    KOiK02981.
    OMAiVYTQSKG.
    OrthoDBiEOG7P5T1Q.
    PhylomeDBiP15880.
    TreeFamiTF300806.

    Family and domain databases

    Gene3Di3.30.160.20. 1 hit.
    3.30.230.10. 1 hit.
    InterProiIPR014720. dsRNA-bd_dom.
    IPR000851. Ribosomal_S5.
    IPR005324. Ribosomal_S5_C.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    IPR005711. Ribosomal_S5_euk/arc.
    IPR013810. Ribosomal_S5_N.
    IPR018192. Ribosomal_S5_N_CS.
    [Graphical view]
    PANTHERiPTHR13718. PTHR13718. 1 hit.
    PfamiPF00333. Ribosomal_S5. 1 hit.
    PF03719. Ribosomal_S5_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF54211. SSF54211. 1 hit.
    TIGRFAMsiTIGR01020. rpsE_arch. 1 hit.
    PROSITEiPS00585. RIBOSOMAL_S5. 1 hit.
    PS50881. S5_DSRBD. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P15880-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADDAGAAGG PGGPGGPGMG NRGGFRGGFG SGIRGRGRGR GRGRGRGRGA    50
    RGGKAEDKEW MPVTKLGRLV KDMKIKSLEE IYLFSLPIKE SEIIDFFLGA 100
    SLKDEVLKIM PVQKQTRAGQ RTRFKAFVAI GDYNGHVGLG VKCSKEVATA 150
    IRGAIILAKL SIVPVRRGYW GNKIGKPHTV PCKVTGRCGS VLVRLIPAPR 200
    GTGIVSAPVP KKLLMMAGID DCYTSARGCT ATLGNFAKAT FDAISKTYSY 250
    LTPDLWKETV FTKSPYQEFT DHLVKTHTRV SVQRTQAPAV ATT 293
    Length:293
    Mass (Da):31,324
    Last modified:October 1, 1996 - v2
    Checksum:i66C0DB7ED393B036
    GO

    Sequence cautioni

    The sequence CAA35078.1 differs from that shown. Reason: Frameshift at positions 14, 27, 40, 46, 48 and 52.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X17206 mRNA. Translation: CAA35078.1. Frameshift.
    AK312173 mRNA. Translation: BAG35107.1.
    CH471112 Genomic DNA. Translation: EAW85592.1.
    CH471112 Genomic DNA. Translation: EAW85595.1.
    BC001795 mRNA. Translation: AAH01795.1.
    BC006559 mRNA. Translation: AAH06559.1.
    BC008862 mRNA. Translation: AAH08862.1.
    BC010165 mRNA. Translation: AAH10165.1.
    BC012354 mRNA. Translation: AAH12354.1.
    BC016178 mRNA. Translation: AAH16178.1.
    BC016951 mRNA. Translation: AAH16951.1.
    BC018993 mRNA. Translation: AAH18993.1.
    BC021545 mRNA. Translation: AAH21545.1.
    BC023541 mRNA. Translation: AAH23541.1.
    BC025677 mRNA. Translation: AAH25677.1.
    BC066321 mRNA. Translation: AAH66321.1.
    BC068051 mRNA. Translation: AAH68051.1.
    BC071922 mRNA. Translation: AAH71922.1.
    BC071923 mRNA. Translation: AAH71923.1.
    BC071924 mRNA. Translation: AAH71924.1.
    BC073966 mRNA. Translation: AAH73966.1.
    BC075830 mRNA. Translation: AAH75830.1.
    BC103756 mRNA. Translation: AAI03757.1.
    BC105985 mRNA. Translation: AAI05986.1.
    CCDSiCCDS10452.1.
    PIRiS08228.
    RefSeqiNP_002943.2. NM_002952.3.
    UniGeneiHs.356366.
    Hs.381079.
    Hs.498569.
    Hs.506997.

    Genome annotation databases

    EnsembliENST00000343262; ENSP00000341885; ENSG00000140988.
    GeneIDi6187.
    KEGGihsa:6187.
    UCSCiuc002cnn.2. human.

    Polymorphism databases

    DMDMi1710756.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X17206 mRNA. Translation: CAA35078.1 . Frameshift.
    AK312173 mRNA. Translation: BAG35107.1 .
    CH471112 Genomic DNA. Translation: EAW85592.1 .
    CH471112 Genomic DNA. Translation: EAW85595.1 .
    BC001795 mRNA. Translation: AAH01795.1 .
    BC006559 mRNA. Translation: AAH06559.1 .
    BC008862 mRNA. Translation: AAH08862.1 .
    BC010165 mRNA. Translation: AAH10165.1 .
    BC012354 mRNA. Translation: AAH12354.1 .
    BC016178 mRNA. Translation: AAH16178.1 .
    BC016951 mRNA. Translation: AAH16951.1 .
    BC018993 mRNA. Translation: AAH18993.1 .
    BC021545 mRNA. Translation: AAH21545.1 .
    BC023541 mRNA. Translation: AAH23541.1 .
    BC025677 mRNA. Translation: AAH25677.1 .
    BC066321 mRNA. Translation: AAH66321.1 .
    BC068051 mRNA. Translation: AAH68051.1 .
    BC071922 mRNA. Translation: AAH71922.1 .
    BC071923 mRNA. Translation: AAH71923.1 .
    BC071924 mRNA. Translation: AAH71924.1 .
    BC073966 mRNA. Translation: AAH73966.1 .
    BC075830 mRNA. Translation: AAH75830.1 .
    BC103756 mRNA. Translation: AAI03757.1 .
    BC105985 mRNA. Translation: AAI05986.1 .
    CCDSi CCDS10452.1.
    PIRi S08228.
    RefSeqi NP_002943.2. NM_002952.3.
    UniGenei Hs.356366.
    Hs.381079.
    Hs.498569.
    Hs.506997.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3J3A electron microscopy 5.00 C 1-293 [» ]
    ProteinModelPortali P15880.
    SMRi P15880. Positions 53-278.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112101. 169 interactions.
    IntActi P15880. 32 interactions.
    MINTi MINT-3008399.
    STRINGi 9606.ENSP00000341885.

    PTM databases

    PhosphoSitei P15880.

    Polymorphism databases

    DMDMi 1710756.

    Proteomic databases

    MaxQBi P15880.
    PaxDbi P15880.
    PRIDEi P15880.

    Protocols and materials databases

    DNASUi 6187.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000343262 ; ENSP00000341885 ; ENSG00000140988 .
    GeneIDi 6187.
    KEGGi hsa:6187.
    UCSCi uc002cnn.2. human.

    Organism-specific databases

    CTDi 6187.
    GeneCardsi GC16M002012.
    H-InvDB HIX0029256.
    HIX0039223.
    HIX0202579.
    HGNCi HGNC:10404. RPS2.
    HPAi HPA055133.
    MIMi 603624. gene.
    neXtProti NX_P15880.
    PharmGKBi PA34806.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0098.
    HOGENOMi HOG000072596.
    HOVERGENi HBG000437.
    InParanoidi P15880.
    KOi K02981.
    OMAi VYTQSKG.
    OrthoDBi EOG7P5T1Q.
    PhylomeDBi P15880.
    TreeFami TF300806.

    Enzyme and pathway databases

    Reactomei REACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
    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_1979. Translation initiation complex formation.
    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_931. Ribosomal scanning and start codon recognition.
    REACT_9491. Viral mRNA Translation.

    Miscellaneous databases

    GeneWikii RPS2.
    GenomeRNAii 6187.
    NextBioi 24025.
    PROi P15880.
    SOURCEi Search...

    Gene expression databases

    Bgeei P15880.
    CleanExi HS_RPS2.
    Genevestigatori P15880.

    Family and domain databases

    Gene3Di 3.30.160.20. 1 hit.
    3.30.230.10. 1 hit.
    InterProi IPR014720. dsRNA-bd_dom.
    IPR000851. Ribosomal_S5.
    IPR005324. Ribosomal_S5_C.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    IPR005711. Ribosomal_S5_euk/arc.
    IPR013810. Ribosomal_S5_N.
    IPR018192. Ribosomal_S5_N_CS.
    [Graphical view ]
    PANTHERi PTHR13718. PTHR13718. 1 hit.
    Pfami PF00333. Ribosomal_S5. 1 hit.
    PF03719. Ribosomal_S5_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54211. SSF54211. 1 hit.
    TIGRFAMsi TIGR01020. rpsE_arch. 1 hit.
    PROSITEi PS00585. RIBOSOMAL_S5. 1 hit.
    PS50881. S5_DSRBD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human cDNA sequence homologous to the mouse LLRep3 gene family."
      Slynn G., Jenner D., Potts W., Elvin P., Morten J.E.N., Markham A.F.
      Nucleic Acids Res. 18:681-681(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Colon.
    2. "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.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE 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].
      Tissue: Brain, Cervix, Colon, Eye, Kidney, Lung, Mammary gland, Muscle, Placenta, Skin, Testis and Uterus.
    5. "Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry."
      Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.
      Eur. J. Biochem. 239:144-149(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 276-291.
      Tissue: Placenta.
    6. "Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3)."
      Swiercz R., Person M.D., Bedford M.T.
      Biochem. J. 386:85-91(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION BY PRMT3.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    9. "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-263 AND LYS-275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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-264 AND SER-281, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Discovery of peptidylarginine deiminase-4 substrates by protein array: antagonistic citrullination and methylation of human ribosomal protein S2."
      Guo Q., Bedford M.T., Fast W.
      Mol. Biosyst. 7:2286-2295(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: CITRULLINATION.
    13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    14. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

    Entry informationi

    Entry nameiRS2_HUMAN
    AccessioniPrimary (citable) accession number: P15880
    Secondary accession number(s): B2R5G0, D3DU82, Q3MIB1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 159 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

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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