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Protein

40S ribosomal protein S30

Gene

FAU

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

Functioni

GO - Molecular functioni

  1. RNA binding Source: ProtInc
  2. structural constituent of ribosome Source: UniProtKB

GO - Biological processi

  1. antibacterial humoral response Source: UniProtKB
  2. cellular protein metabolic process Source: Reactome
  3. defense response to Gram-positive bacterium Source: UniProtKB
  4. gene expression Source: Reactome
  5. innate immune response in mucosa Source: UniProtKB
  6. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay 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
Complete GO annotation...

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 S30
Gene namesi
Name:FAU
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:3597. FAU.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. cytosolic small ribosomal subunit Source: UniProtKB
  3. extracellular space Source: UniProtKB
  4. small ribosomal subunit Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 595940S ribosomal protein S30PRO_0000173999Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511N6-succinyllysineBy similarity

Proteomic databases

MaxQBiP62861.
PaxDbiP62861.
PRIDEiP62861.

PTM databases

PhosphoSiteiP62861.

Expressioni

Gene expression databases

BgeeiP62861.
CleanExiHS_FAU.
ExpressionAtlasiP62861. baseline and differential.
GenevestigatoriP62861.

Organism-specific databases

HPAiHPA059015.

Interactioni

Protein-protein interaction databases

IntActiP62861. 8 interactions.
MINTiMINT-5001188.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00Ae1-59[»]
SMRiP62861. Positions 3-59.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S30e family.Curated

Phylogenomic databases

eggNOGiNOG285974.
HOGENOMiHOG000233941.
HOVERGENiHBG000057.
OrthoDBiEOG7TTQ9R.

Family and domain databases

InterProiIPR006846. Ribosomal_S30.
[Graphical view]
PfamiPF04758. Ribosomal_S30. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P62861-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
KVHGSLARAG KVRGQTPKVA KQEKKKKKTG RAKRRMQYNR RFVNVVPTFG

KKKGPNANS
Length:59
Mass (Da):6,648
Last modified:August 16, 2004 - v1
Checksum:i012AC1FB555B01A4
GO

Sequence cautioni

The sequence AAH33877.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAQ87877.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB15515.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA46714.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA46716.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAG46772.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti19 – 191V → M.1 Publication
VAR_019643

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65921 Genomic DNA. Translation: CAA46714.1. Different initiation.
X65923 mRNA. Translation: CAA46716.1. Different initiation.
AK026639 mRNA. Translation: BAB15515.1. Different initiation.
CR541974 mRNA. Translation: CAG46772.1. Different initiation.
AY398663 Genomic DNA. Translation: AAQ87877.1. Different initiation.
AP003068 Genomic DNA. No translation available.
BC033877 mRNA. Translation: AAH33877.1. Different initiation.
PIRiJC1278.
UniGeneiHs.387208.

Genome annotation databases

EnsembliENST00000527548; ENSP00000434440; ENSG00000149806.
ENST00000529639; ENSP00000435370; ENSG00000149806.
ENST00000531743; ENSP00000431822; ENSG00000149806.

Polymorphism databases

DMDMi51338655.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65921 Genomic DNA. Translation: CAA46714.1. Different initiation.
X65923 mRNA. Translation: CAA46716.1. Different initiation.
AK026639 mRNA. Translation: BAB15515.1. Different initiation.
CR541974 mRNA. Translation: CAG46772.1. Different initiation.
AY398663 Genomic DNA. Translation: AAQ87877.1. Different initiation.
AP003068 Genomic DNA. No translation available.
BC033877 mRNA. Translation: AAH33877.1. Different initiation.
PIRiJC1278.
UniGeneiHs.387208.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00Ae1-59[»]
SMRiP62861. Positions 3-59.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP62861. 8 interactions.
MINTiMINT-5001188.

PTM databases

PhosphoSiteiP62861.

Polymorphism databases

DMDMi51338655.

Proteomic databases

MaxQBiP62861.
PaxDbiP62861.
PRIDEiP62861.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000527548; ENSP00000434440; ENSG00000149806.
ENST00000529639; ENSP00000435370; ENSG00000149806.
ENST00000531743; ENSP00000431822; ENSG00000149806.

Organism-specific databases

GeneCardsiGC11M064888.
HGNCiHGNC:3597. FAU.
HPAiHPA059015.
MIMi134690. gene.
neXtProtiNX_P62861.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG285974.
HOGENOMiHOG000233941.
HOVERGENiHBG000057.
OrthoDBiEOG7TTQ9R.

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.

Miscellaneous databases

ChiTaRSiFAU. human.
SOURCEiSearch...

Gene expression databases

BgeeiP62861.
CleanExiHS_FAU.
ExpressionAtlasiP62861. baseline and differential.
GenevestigatoriP62861.

Family and domain databases

InterProiIPR006846. Ribosomal_S30.
[Graphical view]
PfamiPF04758. Ribosomal_S30. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genomic structure and expression of the human fau gene: encoding the ribosomal protein S30 fused to a ubiquitin-like protein."
    Kas K., Michiels L., Merregaert J.
    Biochem. Biophys. Res. Commun. 187:927-933(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "fau cDNA encodes a ubiquitin-like-S30 fusion protein and is expressed as an antisense sequence in the Finkel-Biskis-Reilly murine sarcoma virus."
    Michiels L., van der Rauwelaert E., van Hasselt F., Kas K., Merregaert J.
    Oncogene 8:2537-2546(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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(2003) [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)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. NIEHS SNPs program
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-19.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon.
  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(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-25.
    Tissue: Placenta.
  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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRS30_HUMAN
AccessioniPrimary (citable) accession number: P62861
Secondary accession number(s): Q05472, Q95261, Q9H5V4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: April 1, 2015
This is version 96 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

Miscellaneous

This ribosomal protein is synthesized as a C-terminal extension protein (CEP) of a ubiquitin-like protein.

Keywords - Technical termi

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

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Ribosomal proteins
    Ribosomal proteins families and list of entries
  7. 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.