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P62081 (RS7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
40S ribosomal protein S7
Gene names
Name:RPS7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length194 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for rRNA maturation. Ref.8

Subunit structure

Binds IPO9 with high affinity. Interacts with NEK6. Ref.7 Ref.12

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Note: Colocalizes with NEK6 in the centrosome. Ref.12

Post-translational modification

Phosphorylated by NEK6. Ref.12

Involvement in disease

Diamond-Blackfan anemia 8 (DBA8) [MIM:612563]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8

Sequence similarities

Belongs to the ribosomal protein S7e family.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   DiseaseDiamond-Blackfan anemia
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

SRP-dependent cotranslational protein targeting to membrane

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Traceable author statement. Source: Reactome

rRNA processing

Inferred from mutant phenotype PubMed 18697920. Source: UniProtKB

ribosomal small subunit biogenesis

Inferred from mutant phenotype PubMed 18697920. Source: UniProtKB

translation

Non-traceable author statement Ref.1. Source: UniProtKB

translational elongation

Traceable author statement. Source: Reactome

translational initiation

Traceable author statement. Source: Reactome

translational termination

Traceable author statement. Source: Reactome

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

viral transcription

Traceable author statement. Source: Reactome

   Cellular_component90S preribosome

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

cytosolic small ribosomal subunit

Inferred from direct assay PubMed 15883184Ref.6. Source: UniProtKB

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from direct assay Ref.7. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 9687515. Source: UniProtKB

ribonucleoprotein complex

Inferred from direct assay PubMed 18809582. Source: MGI

ribosome

Inferred from direct assay PubMed 15883184. Source: UniProtKB

small-subunit processome

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionRNA binding

Non-traceable author statement Ref.1. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

structural constituent of ribosome

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MDM2Q0098715EBI-354360,EBI-389668
NEDD8Q158432EBI-354360,EBI-716247

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 19419440S ribosomal protein S7
PRO_0000174190

Regions

Compositional bias98 – 12023Arg/Lys-rich (basic)

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue741N6-acetyllysine Ref.11

Sequences

Sequence LengthMass (Da)Tools
P62081 [UniParc].

Last modified June 21, 2004. Version 1.
Checksum: E21089929CC061E9

FASTA19422,127
        10         20         30         40         50         60 
MFSSSAKIVK PNGEKPDEFE SGISQALLEL EMNSDLKAQL RELNITAAKE IEVGGGRKAI 

        70         80         90        100        110        120 
IIFVPVPQLK SFQKIQVRLV RELEKKFSGK HVVFIAQRRI LPKPTRKSRT KNKQKRPRSR 

       130        140        150        160        170        180 
TLTAVHDAIL EDLVFPSEIV GKRIRVKLDG SRLIKVHLDK AQQNNVEHKV ETFSGVYKKL 

       190 
TGKDVNFEFP EFQL 

« Hide

References

« Hide 'large scale' references
[1]"The human ribosomal protein S7-encoding gene: isolation, structure and localization in 2p25."
Annilo T., Laan M., Stahl J., Metspalu A.
Gene 165:297-302(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[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. expand/collapse author list , 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: Spleen.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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, Liver and Lung.
[6]"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 170-177.
Tissue: Placenta.
[7]"Importins fulfill a dual function as nuclear import receptors and cytoplasmic chaperones for exposed basic domains."
Jaekel S., Mingot J.-M., Schwarzmaier P., Hartmann E., Goerlich D.
EMBO J. 21:377-386(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IPO9.
[8]"Ribosomal protein L5 and L11 mutations are associated with cleft palate and abnormal thumbs in Diamond-Blackfan anemia patients."
Gazda H.T., Sheen M.R., Vlachos A., Choesmel V., O'Donohue M.-F., Schneider H., Darras N., Hasman C., Sieff C.A., Newburger P.E., Ball S.E., Niewiadomska E., Matysiak M., Zaucha J.M., Glader B., Niemeyer C., Meerpohl J.J., Atsidaftos E. expand/collapse author list , Lipton J.M., Gleizes P.-E., Beggs A.H.
Am. J. Hum. Genet. 83:769-780(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INVOLVEMENT IN DBA8.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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.
[11]"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-74, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Characterization of hNek6 interactome reveals an important role for its short N-terminal domain and colocalization with proteins at the centrosome."
Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C., Santana Bernachi J., Paes Leme A.F., Kobarg J.
J. Proteome Res. 9:6298-6316(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NEK6, PHOSPHORYLATION BY NEK6.
[13]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Structures of the human and Drosophila 80S ribosome."
Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M., Wilson D.N., Beckmann R.
Nature 497:80-85(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJC4388.
RefSeqNP_001002.1. NM_001011.3.
UniGeneHs.534346.
Hs.546287.
Hs.646582.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Aelectron microscopy5.00H1-194[»]
ProteinModelPortalP62081.
SMRP62081. Positions 5-194.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112115. 128 interactions.
IntActP62081. 20 interactions.
MINTMINT-5001160.
STRING9606.ENSP00000339095.

PTM databases

PhosphoSiteP62081.

Polymorphism databases

DMDM49065831.

Proteomic databases

PaxDbP62081.
PeptideAtlasP62081.
PRIDEP62081.

Protocols and materials databases

DNASU6201.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000304921; ENSP00000339095; ENSG00000171863.
ENST00000403564; ENSP00000385018; ENSG00000171863.
ENST00000406376; ENSP00000385286; ENSG00000171863.
GeneID6201.
KEGGhsa:6201.
UCSCuc002qxw.3. human.

Organism-specific databases

CTD6201.
GeneCardsGC02P003622.
HGNCHGNC:10440. RPS7.
HPAHPA056586.
MIM603658. gene.
612563. phenotype.
neXtProtNX_P62081.
Orphanet124. Blackfan-Diamond anemia.
PharmGKBPA34855.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG280542.
HOGENOMHOG000197237.
HOVERGENHBG001698.
InParanoidP62081.
KOK02993.
OMAIEVGHGK.
OrthoDBEOG74J997.
PhylomeDBP62081.
TreeFamTF343364.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

BgeeP62081.
CleanExHS_RPS7.
GenevestigatorP62081.

Family and domain databases

InterProIPR000554. Ribosomal_S7e.
[Graphical view]
PANTHERPTHR11278. PTHR11278. 1 hit.
PfamPF01251. Ribosomal_S7e. 1 hit.
[Graphical view]
PROSITEPS00948. RIBOSOMAL_S7E. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPS7. human.
GeneWikiRPS7.
GenomeRNAi6201.
NextBio24083.
PMAP-CutDBP62081.
PROP62081.
SOURCESearch...

Entry information

Entry nameRS7_HUMAN
AccessionPrimary (citable) accession number: P62081
Secondary accession number(s): P23821 expand/collapse secondary AC list , P24818, Q57Z92, Q6IPH1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: June 21, 2004
Last modified: April 16, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM