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P42677

- RS27_HUMAN

UniProt

P42677 - RS27_HUMAN

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Protein
40S ribosomal protein S27
Gene
RPS27, MPS1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Cofactori

Binds 1 zinc ion per subunit Reviewed prediction.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri37 – 5923C4-type Reviewed prediction
Add
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. RNA metabolic process Source: Reactome
  2. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  3. cell proliferation Source: UniProtKB
  4. cellular protein metabolic process Source: Reactome
  5. gene expression Source: Reactome
  6. mRNA metabolic process Source: Reactome
  7. mitotic cell cycle Source: Reactome
  8. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay 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
Complete GO annotation...

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
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34820.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 848340S ribosomal protein S27UniRule annotation
PRO_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.

Family & Domainsi

Sequence similaritiesi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51K → R AA sequence 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 150 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 (1 Publication) 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.

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

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