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Protein

40S ribosomal protein S7

Gene

RPS7

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

Functioni

Required for rRNA maturation.1 Publication

GO - Molecular functioni

  • mRNA 3'-UTR binding Source: CAFA
  • mRNA 5'-UTR binding Source: CAFA
  • protein kinase binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • structural constituent of ribosome Source: InterPro
  • ubiquitin ligase inhibitor activity Source: CAFA

GO - Biological processi

  • cytoplasmic translation Source: GO_Central
  • negative regulation of ubiquitin-dependent protein catabolic process Source: CAFA
  • negative regulation of ubiquitin protein ligase activity Source: CAFA
  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  • positive regulation of gene expression Source: CAFA
  • positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator Source: CAFA
  • protein stabilization Source: CAFA
  • ribosomal small subunit biogenesis Source: UniProtKB
  • rRNA processing Source: UniProtKB
  • SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  • translation Source: UniProtKB
  • translational initiation Source: Reactome

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiR-HSA-156827 L13a-mediated translational silencing of Ceruloplasmin expression
R-HSA-156902 Peptide chain elongation
R-HSA-1799339 SRP-dependent cotranslational protein targeting to membrane
R-HSA-192823 Viral mRNA Translation
R-HSA-2408557 Selenocysteine synthesis
R-HSA-6790901 rRNA modification in the nucleus and cytosol
R-HSA-6791226 Major pathway of rRNA processing in the nucleolus and cytosol
R-HSA-72649 Translation initiation complex formation
R-HSA-72689 Formation of a pool of free 40S subunits
R-HSA-72695 Formation of the ternary complex, and subsequently, the 43S complex
R-HSA-72702 Ribosomal scanning and start codon recognition
R-HSA-72706 GTP hydrolysis and joining of the 60S ribosomal subunit
R-HSA-72764 Eukaryotic Translation Termination
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-975956 Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)
R-HSA-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

Protein family/group databases

MoonProtiP62081

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S7
Alternative name(s):
Small ribosomal subunit protein eS71 Publication
Gene namesi
Name:RPS7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi

Organism-specific databases

EuPathDBiHostDB:ENSG00000171863.12
HGNCiHGNC:10440 RPS7
MIMi603658 gene
neXtProtiNX_P62081

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Diamond-Blackfan anemia 8 (DBA8)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of malignancy. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies.
See also OMIM:612563

Keywords - Diseasei

Diamond-Blackfan anemia

Organism-specific databases

DisGeNETi6201
GeneReviewsiRPS7
MalaCardsiRPS7
MIMi612563 phenotype
OpenTargetsiENSG00000171863
Orphaneti124 Blackfan-Diamond anemia
PharmGKBiPA34855

Polymorphism and mutation databases

BioMutaiRPS7
DMDMi49065831

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001741901 – 19440S ribosomal protein S7Add BLAST194

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Cross-linki70Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei74N6-acetyllysine; alternateCombined sources1
Cross-linki74Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources

Post-translational modificationi

Phosphorylated by NEK6.1 Publication
Ubiquitinated. Deubiquitinated by DESI2, leading to its stabilization.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiP62081
PaxDbiP62081
PeptideAtlasiP62081
PRIDEiP62081
TopDownProteomicsiP62081

PTM databases

iPTMnetiP62081
PhosphoSitePlusiP62081
SwissPalmiP62081

Miscellaneous databases

PMAP-CutDBiP62081

Expressioni

Gene expression databases

BgeeiENSG00000171863
CleanExiHS_RPS7
ExpressionAtlasiP62081 baseline and differential
GenevisibleiP62081 HS

Organism-specific databases

HPAiHPA056586

Interactioni

Subunit structurei

Binds IPO9 with high affinity (PubMed:11823430). Interacts with NEK6 (PubMed:20873783). Interacts with DESI2 (PubMed:28483520).3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112115, 182 interactors
CORUMiP62081
IntActiP62081, 35 interactors
MINTiP62081
STRINGi9606.ENSP00000339095

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4UG0electron microscopy-SH1-194[»]
4V6Xelectron microscopy5.00AH1-194[»]
5A2Qelectron microscopy3.90H1-194[»]
5AJ0electron microscopy3.50BH1-194[»]
5FLXelectron microscopy3.90H1-194[»]
5LKSelectron microscopy3.60SH1-194[»]
5OA3electron microscopy4.30H1-194[»]
5T2Celectron microscopy3.60At1-194[»]
5VYCX-ray6.00H1/H2/H3/H4/H5/H61-194[»]
6EK0electron microscopy2.90SH1-194[»]
6FECelectron microscopy6.30X5-194[»]
ProteinModelPortaliP62081
SMRiP62081
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi98 – 120Arg/Lys-rich (basic)Add BLAST23

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3320 Eukaryota
ENOG410ZYKB LUCA
GeneTreeiENSGT00390000014122
HOGENOMiHOG000197237
HOVERGENiHBG001698
InParanoidiP62081
KOiK02993
OMAiGFHRVQQ
OrthoDBiEOG091G0L94
PhylomeDBiP62081
TreeFamiTF343364

Family and domain databases

InterProiView protein in InterPro
IPR000554 Ribosomal_S7e
PANTHERiPTHR11278 PTHR11278, 1 hit
PfamiView protein in Pfam
PF01251 Ribosomal_S7e, 1 hit
PROSITEiView protein in PROSITE
PS00948 RIBOSOMAL_S7E, 1 hit

Sequencei

Sequence statusi: Complete.

P62081-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFSSSAKIVK PNGEKPDEFE SGISQALLEL EMNSDLKAQL RELNITAAKE
60 70 80 90 100
IEVGGGRKAI IIFVPVPQLK SFQKIQVRLV RELEKKFSGK HVVFIAQRRI
110 120 130 140 150
LPKPTRKSRT KNKQKRPRSR TLTAVHDAIL EDLVFPSEIV GKRIRVKLDG
160 170 180 190
SRLIKVHLDK AQQNNVEHKV ETFSGVYKKL TGKDVNFEFP EFQL
Length:194
Mass (Da):22,127
Last modified:June 21, 2004 - v1
Checksum:iE21089929CC061E9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77233 mRNA Translation: AAB00969.1
Z25749 Genomic DNA Translation: CAA81022.1
AK311794 mRNA Translation: BAG34737.1
AC108488 Genomic DNA Translation: AAX82027.1
CH471053 Genomic DNA Translation: EAX01057.1
CH471053 Genomic DNA Translation: EAX01058.1
CH471053 Genomic DNA Translation: EAX01059.1
BC002866 mRNA Translation: AAH02866.1
BC061901 mRNA Translation: AAH61901.1
BC071919 mRNA Translation: AAH71919.1
CCDSiCCDS1648.1
PIRiJC4388
RefSeqiNP_001002.1, NM_001011.3
UniGeneiHs.534346
Hs.546287
Hs.646582

Genome annotation databases

EnsembliENST00000304921; ENSP00000339095; ENSG00000171863
ENST00000403564; ENSP00000385018; ENSG00000171863
ENST00000406376; ENSP00000385286; ENSG00000171863
GeneIDi6201
KEGGihsa:6201
UCSCiuc002qxw.4 human

Entry informationi

Entry nameiRS7_HUMAN
AccessioniPrimary (citable) accession number: P62081
Secondary accession number(s): P23821
, P24818, Q57Z92, Q6IPH1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: June 21, 2004
Last modified: May 23, 2018
This is version 146 of the entry and version 1 of the sequence. See 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 2
    Human chromosome 2: 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

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