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P42677

- RS27_HUMAN

UniProt

P42677 - RS27_HUMAN

Protein

40S ribosomal protein S27

Gene

RPS27

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

    Cofactori

    Binds 1 zinc ion per subunit.Curated

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri37 – 5923C4-typeSequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. structural constituent of ribosome Source: InterPro
    5. zinc ion binding Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Ligandi

    Metal-binding, Zinc

    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_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    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_682. Mitotic Prometaphase.
    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 S27
    Alternative name(s):
    Metallopan-stimulin 1
    Short name:
    MPS-1
    Gene namesi
    Name:RPS27
    Synonyms:MPS1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:10416. RPS27.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. cytosolic small ribosomal subunit Source: UniProtKB
    3. nucleus Source: UniProtKB
    4. ribosome Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34820.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 848340S ribosomal protein S27PRO_0000149051Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei11 – 111Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP42677.
    PaxDbiP42677.
    PRIDEiP42677.

    PTM databases

    PhosphoSiteiP42677.

    Expressioni

    Tissue specificityi

    Expressed in a wide variety of actively proliferating cells and tumor tissues.

    Gene expression databases

    BgeeiP42677.
    CleanExiHS_RPS27.
    GenevestigatoriP42677.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LRRK2Q5S0072EBI-356336,EBI-5323863
    MDM2Q009875EBI-356336,EBI-389668

    Protein-protein interaction databases

    BioGridi112146. 68 interactions.
    IntActiP42677. 25 interactions.
    MINTiMINT-5004996.
    STRINGi9606.ENSP00000357555.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Aelectron microscopy5.00b1-84[»]
    ProteinModelPortaliP42677.
    SMRiP42677. Positions 1-84.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein S27e family.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri37 – 5923C4-typeSequence AnalysisAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG2051.
    HOVERGENiHBG000252.
    InParanoidiP42677.
    KOiK02978.
    OMAiCASVLCQ.
    OrthoDBiEOG78SQM9.
    PhylomeDBiP42677.
    TreeFamiTF300265.

    Family and domain databases

    Gene3Di2.20.25.100. 1 hit.
    HAMAPiMF_00371. Ribosomal_S27e.
    InterProiIPR000592. Ribosomal_S27e.
    IPR023407. Ribosomal_S27e_Zn-bd_dom.
    IPR011332. Ribosomal_zn-bd.
    [Graphical view]
    PANTHERiPTHR11594. PTHR11594. 1 hit.
    PfamiPF01667. Ribosomal_S27e. 1 hit.
    [Graphical view]
    ProDomiPD004466. Ribosomal_S27e. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF57829. SSF57829. 1 hit.
    PROSITEiPS01168. RIBOSOMAL_S27E. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P42677-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPLAKDLLHP SPEEEKRKHK KKRLVQSPNS YFMDVKCPGC YKITTVFSHA   50
    QTVVLCVGCS TVLCQPTGGK ARLTEGCSFR RKQH 84
    Length:84
    Mass (Da):9,461
    Last modified:January 23, 2007 - v3
    Checksum:i242C4466AC8A8900
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51K → R AA sequence (PubMed:8706699)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L19739 mRNA. Translation: AAA59867.1.
    U57847 mRNA. Translation: AAB02266.1.
    AB061845 Genomic DNA. Translation: BAB79483.1.
    AK312070 mRNA. Translation: BAG35006.1.
    AL358472 Genomic DNA. Translation: CAI14033.1.
    CH471121 Genomic DNA. Translation: EAW53239.1.
    CH471055 Genomic DNA. Translation: EAW64624.1.
    CH471116 Genomic DNA. Translation: EAW88871.1.
    BC002658 mRNA. Translation: AAH02658.1.
    BC070219 mRNA. Translation: AAH70219.1.
    AB007162 Genomic DNA. Translation: BAA25825.1.
    CCDSiCCDS1059.1.
    PIRiA48045.
    RefSeqiNP_001021.1. NM_001030.4.
    UniGeneiHs.546291.
    Hs.654475.

    Genome annotation databases

    EnsembliENST00000368567; ENSP00000357555; ENSG00000177954.
    GeneIDi6232.
    KEGGihsa:6232.
    UCSCiuc001fdv.3. human.

    Polymorphism databases

    DMDMi1171014.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L19739 mRNA. Translation: AAA59867.1 .
    U57847 mRNA. Translation: AAB02266.1 .
    AB061845 Genomic DNA. Translation: BAB79483.1 .
    AK312070 mRNA. Translation: BAG35006.1 .
    AL358472 Genomic DNA. Translation: CAI14033.1 .
    CH471121 Genomic DNA. Translation: EAW53239.1 .
    CH471055 Genomic DNA. Translation: EAW64624.1 .
    CH471116 Genomic DNA. Translation: EAW88871.1 .
    BC002658 mRNA. Translation: AAH02658.1 .
    BC070219 mRNA. Translation: AAH70219.1 .
    AB007162 Genomic DNA. Translation: BAA25825.1 .
    CCDSi CCDS1059.1.
    PIRi A48045.
    RefSeqi NP_001021.1. NM_001030.4.
    UniGenei Hs.546291.
    Hs.654475.

    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 b 1-84 [» ]
    ProteinModelPortali P42677.
    SMRi P42677. Positions 1-84.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112146. 68 interactions.
    IntActi P42677. 25 interactions.
    MINTi MINT-5004996.
    STRINGi 9606.ENSP00000357555.

    Chemistry

    BindingDBi P42677.
    ChEMBLi CHEMBL1932893.

    PTM databases

    PhosphoSitei P42677.

    Polymorphism databases

    DMDMi 1171014.

    Proteomic databases

    MaxQBi P42677.
    PaxDbi P42677.
    PRIDEi P42677.

    Protocols and materials databases

    DNASUi 6232.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368567 ; ENSP00000357555 ; ENSG00000177954 .
    GeneIDi 6232.
    KEGGi hsa:6232.
    UCSCi uc001fdv.3. human.

    Organism-specific databases

    CTDi 6232.
    GeneCardsi GC01P153963.
    H-InvDB HIX0033569.
    HIX0164279.
    HGNCi HGNC:10416. RPS27.
    MIMi 603702. gene.
    neXtProti NX_P42677.
    PharmGKBi PA34820.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2051.
    HOVERGENi HBG000252.
    InParanoidi P42677.
    KOi K02978.
    OMAi CASVLCQ.
    OrthoDBi EOG78SQM9.
    PhylomeDBi P42677.
    TreeFami TF300265.

    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_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    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_682. Mitotic Prometaphase.
    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

    ChiTaRSi RpS27. human.
    GeneWikii RPS27.
    GenomeRNAii 6232.
    NextBioi 24193.
    PROi P42677.
    SOURCEi Search...

    Gene expression databases

    Bgeei P42677.
    CleanExi HS_RPS27.
    Genevestigatori P42677.

    Family and domain databases

    Gene3Di 2.20.25.100. 1 hit.
    HAMAPi MF_00371. Ribosomal_S27e.
    InterProi IPR000592. Ribosomal_S27e.
    IPR023407. Ribosomal_S27e_Zn-bd_dom.
    IPR011332. Ribosomal_zn-bd.
    [Graphical view ]
    PANTHERi PTHR11594. PTHR11594. 1 hit.
    Pfami PF01667. Ribosomal_S27e. 1 hit.
    [Graphical view ]
    ProDomi PD004466. Ribosomal_S27e. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF57829. SSF57829. 1 hit.
    PROSITEi PS01168. RIBOSOMAL_S27E. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A growth factor-inducible gene encodes a novel nuclear protein with zinc finger structure."
      Fernandez-Pol J.A., Klos D.J., Hamilton P.D.
      J. Biol. Chem. 268:21198-21204(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Mammary carcinoma.
    2. "Primary structures and sequence analysis of human ribosomal proteins L39 and S27."
      Tsui S.K.W., Lee S.M.Y., Fung K.P., Waye M.M.Y., Lee C.Y.
      Biochem. Mol. Biol. Int. 40:611-616(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Heart.
    3. "The human ribosomal protein genes: sequencing and comparative analysis of 73 genes."
      Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.
      Genome Res. 12:379-390(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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: Tongue.
    5. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Uterus.
    8. "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 2-11.
    9. "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 6-74.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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-11, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

    Entry informationi

    Entry nameiRS27_HUMAN
    AccessioniPrimary (citable) accession number: P42677
    Secondary accession number(s): Q5T4L6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 151 of the entry and version 3 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

    Caution

    Was originally (PubMed:8407955) thought to be a protein that could have played a role as a potentially important mediator of cellular proliferative responses to various growth factors and other environmental signals. Capable of specific binding to a cAMP response element in DNA.1 Publication

    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