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Protein

40S ribosomal protein S7

Gene

RPS7

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

Functioni

Required for rRNA maturation.1 Publication

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. RNA binding Source: UniProtKB
  3. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. cytoplasmic translation Source: GO_Central
  3. gene expression Source: Reactome
  4. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  5. ribosomal small subunit biogenesis Source: UniProtKB
  6. rRNA processing Source: UniProtKB
  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 S7
Gene namesi
Name:RPS7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:10440. RPS7.

Subcellular locationi

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication
Note: Colocalizes with NEK6 in the centrosome.

GO - Cellular componenti

  1. 90S preribosome Source: GO_Central
  2. cytoplasm Source: HPA
  3. cytosol Source: Reactome
  4. cytosolic small ribosomal subunit Source: UniProtKB
  5. extracellular vesicular exosome Source: UniProtKB
  6. focal adhesion Source: UniProtKB
  7. membrane Source: UniProtKB
  8. microtubule organizing center Source: UniProtKB-SubCell
  9. nucleolus Source: UniProtKB
  10. nucleus Source: UniProtKB
  11. ribonucleoprotein complex Source: MGI
  12. ribosome Source: UniProtKB
  13. small-subunit processome Source: GO_Central
Complete GO annotation...

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

MIMi612563. phenotype.
Orphaneti124. Blackfan-Diamond anemia.
PharmGKBiPA34855.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19419440S ribosomal protein S7PRO_0000174190Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei74 – 741N6-acetyllysine1 Publication

Post-translational modificationi

Phosphorylated by NEK6.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP62081.
PaxDbiP62081.
PeptideAtlasiP62081.
PRIDEiP62081.

PTM databases

PhosphoSiteiP62081.

Miscellaneous databases

PMAP-CutDBP62081.

Expressioni

Gene expression databases

BgeeiP62081.
CleanExiHS_RPS7.
ExpressionAtlasiP62081. baseline and differential.
GenevestigatoriP62081.

Organism-specific databases

HPAiHPA056586.

Interactioni

Subunit structurei

Binds IPO9 with high affinity. Interacts with NEK6.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MDM2Q0098715EBI-354360,EBI-389668
NEDD8Q158432EBI-354360,EBI-716247

Protein-protein interaction databases

BioGridi112115. 132 interactions.
IntActiP62081. 22 interactions.
MINTiMINT-5001160.
STRINGi9606.ENSP00000339095.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AH1-194[»]
ProteinModelPortaliP62081.
SMRiP62081. Positions 5-193.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi98 – 12023Arg/Lys-rich (basic)Add
BLAST

Sequence similaritiesi

Belongs to the ribosomal protein S7e family.Curated

Phylogenomic databases

eggNOGiNOG280542.
GeneTreeiENSGT00390000014122.
HOGENOMiHOG000197237.
HOVERGENiHBG001698.
InParanoidiP62081.
KOiK02993.
OrthoDBiEOG74J997.
PhylomeDBiP62081.
TreeFamiTF343364.

Family and domain databases

InterProiIPR000554. Ribosomal_S7e.
[Graphical view]
PANTHERiPTHR11278. PTHR11278. 1 hit.
PfamiPF01251. Ribosomal_S7e. 1 hit.
[Graphical view]
PROSITEiPS00948. RIBOSOMAL_S7E. 1 hit.
[Graphical view]

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.3. human.

Polymorphism databases

DMDMi49065831.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AH1-194[»]
ProteinModelPortaliP62081.
SMRiP62081. Positions 5-193.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112115. 132 interactions.
IntActiP62081. 22 interactions.
MINTiMINT-5001160.
STRINGi9606.ENSP00000339095.

PTM databases

PhosphoSiteiP62081.

Polymorphism databases

DMDMi49065831.

Proteomic databases

MaxQBiP62081.
PaxDbiP62081.
PeptideAtlasiP62081.
PRIDEiP62081.

Protocols and materials databases

DNASUi6201.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000304921; ENSP00000339095; ENSG00000171863.
ENST00000403564; ENSP00000385018; ENSG00000171863.
ENST00000406376; ENSP00000385286; ENSG00000171863.
GeneIDi6201.
KEGGihsa:6201.
UCSCiuc002qxw.3. human.

Organism-specific databases

CTDi6201.
GeneCardsiGC02P003622.
GeneReviewsiRPS7.
HGNCiHGNC:10440. RPS7.
HPAiHPA056586.
MIMi603658. gene.
612563. phenotype.
neXtProtiNX_P62081.
Orphaneti124. Blackfan-Diamond anemia.
PharmGKBiPA34855.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG280542.
GeneTreeiENSGT00390000014122.
HOGENOMiHOG000197237.
HOVERGENiHBG001698.
InParanoidiP62081.
KOiK02993.
OrthoDBiEOG74J997.
PhylomeDBiP62081.
TreeFamiTF343364.

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

ChiTaRSiRPS7. human.
GeneWikiiRPS7.
GenomeRNAii6201.
NextBioi24083.
PMAP-CutDBP62081.
PROiP62081.
SOURCEiSearch...

Gene expression databases

BgeeiP62081.
CleanExiHS_RPS7.
ExpressionAtlasiP62081. baseline and differential.
GenevestigatoriP62081.

Family and domain databases

InterProiIPR000554. Ribosomal_S7e.
[Graphical view]
PANTHERiPTHR11278. PTHR11278. 1 hit.
PfamiPF01251. Ribosomal_S7e. 1 hit.
[Graphical view]
PROSITEiPS00948. RIBOSOMAL_S7E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1994) [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.
    , 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].
    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.
    , 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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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(2003) [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(1995) [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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IPO9.
  8. Cited for: FUNCTION, INVOLVEMENT IN DBA8.
  9. 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(2008) [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(2008) [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(2009) [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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. 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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.

Entry informationi

Entry nameiRS7_HUMAN
AccessioniPrimary (citable) accession number: P62081
Secondary accession number(s): P23821
, P24818, Q57Z92, Q6IPH1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: June 21, 2004
Last modified: March 4, 2015
This is version 111 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

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

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.