Swiss-Prot Accession Format

The Swiss-Prot Accession Format is a Canonical File Format for Swiss-Prot Records.

• See: PPLRE Swiss-Prot Table, Swissknife.

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References

• http://www.gabormelli.com/images/Swiss-Prot_Accession_Format_Fig1.gif
• http://www.expasy.org/sprot/userman.html
  • Legend

ID Identification One; starts the entry AC Accession number(s) One or more DT Date Three times DE Description One or more GN Gene name(s) Optional OS Organism species One or more OG Organelle Optional OC Organism classification One or more RN Reference number One or more RP Reference position One or more RC Reference comment(s) Optional RX Reference cross-reference(s) Optional RA Reference authors One or more RT Reference title Optional RL Reference location One or more CC Comments or notes Optional DR Database cross-references Optional KW Keywords Optional FT Feature table data Optional SQ Sequence header One

             Amino Acid Sequence               One 

Termination line One; ends the entry

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Detailed Example

General information about the UniProtKB/Swiss-Prot entry Entry name EPO_HUMAN Primary accession number P01588 Secondary accession numbers Q549U2 Q9UDZ0 Q9UEZ5 Q9UHA0 Integrated into UniProtKB/Swiss-Prot 21-JUL-1986 Sequence was last modified     21-JUL-1986, version 1 Entry was last modified 21-MAR-2006, version 68 Protein description Protein name Erythropoietin precursor Synonyms Epoetin Origin of the protein Gene    Gene name  EPO  From Homo sapiens (Human) [TaxID:9606] Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini; Hominidae; Homo. References [1] NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. MEDLINE=85137899; PubMed=3838366;  [NCBI, ExPASy, EBI, Israel, Japan] Jacobs K., Shoemaker C., Rudersdorf R., Neill S.D.,     Kaufman R.J., Mufson A., Seehra J., Jones S.S., Hewick R., Fritsch E.F., Kawakita M., Shimizu T., Miyake T.; "Isolation and characterization of genomic and cDNA clones of human erythropoietin."; Nature 313:806-810(1985). [2] NUCLEOTIDE SEQUENCE [GENOMIC DNA]. MEDLINE=86067948; PubMed=3865178;  [NCBI, ExPASy, EBI, Israel, Japan] Lin F.-K., Suggs S., Lin C.-H., Browne J.K., Smalling R.,     Egrie J.C., Chen K.K., Fox G.M., Martin F., Stabinsky Z., Badrawi S.M., Lai P.-H., Goldwasser E.; "Cloning and expression of the human erythropoietin gene."; Proc. Natl. Acad. Sci. U.S.A. 82:7580-7584(1985). Comments FUNCTION Erythropoietin is the principal hormone involved in the regulation of erythrocyte differentiation and the maintenance of a physiological level of circulating erythrocyte mass. SUBCELLULAR LOCATION Secreted protein. TISSUE SPECIFICITY Produced by kidney or liver of adult mammals and by liver of fetal or neonatal mammals. PHARMACEUTICAL Used for the treatment of anemia. Available under the names Epogen (Amgen), Epogin (Chugai), Epomax (Elanex), Eprex (Janssen-Cilag), NeoRecormon or Recormon (Roche), and Procrit (Ortho Biotech). Variations in the glycosylation pattern of EPO distinguishes these products. Epogen, Epogin, Eprex and Procrit are generically known as epoetin alfa, NeoRecormon and Recormon as epoetin beta and Epomax as epoetin omega. SIMILARITY Belongs to the EPO/TPO family. DATABASE NAME R&D Systems' cytokine source book: EPO WWW "http://www.rndsystems.com/asp/g_sitebuilder.asp?bodyId=197" Cross-references EMBL X02158; CAA26095.1; -; Genomic_DNA. [EMBL/ GenBank/ DDBJ] [CoDingSequence] X02157; CAA26094.1; -; mRNA. [EMBL/ GenBank/ DDBJ] [CoDingSequence] M11319; AAA52400.1; -; Genomic_DNA. [EMBL/ GenBank/ DDBJ] [CoDingSequence] AF053356; AAC78791.1; -; Genomic_DNA. [EMBL/ GenBank/ DDBJ] [CoDingSequence] AF202308; AAF23132.1; -; Genomic_DNA. [EMBL/ GenBank/ DDBJ] [CoDingSequence] AF202306; AAF23132.1; JOINED; Genomic_DNA. [EMBL/ GenBank/ DDBJ] [CoDingSequence] AF202307; AAF23132.1; JOINED; Genomic_DNA. [EMBL/ GenBank/ DDBJ] [CoDingSequence] AF202310; AAF23133.1; -; Genomic_DNA. [EMBL/ GenBank/ DDBJ] [CoDingSequence] AF202309; AAF23133.1; JOINED; Genomic_DNA. [EMBL/ GenBank/ DDBJ] [CoDingSequence] AF202311; AAF17572.1; -; Genomic_DNA. [EMBL/ GenBank/ DDBJ] [CoDingSequence] AF202314; AAF23134.1; -; Genomic_DNA. [EMBL/ GenBank/ DDBJ] [CoDingSequence] AF202312; AAF23134.1; JOINED; Genomic_DNA. [EMBL/ GenBank/ DDBJ] [CoDingSequence] AF202313; AAF23134.1; JOINED; Genomic_DNA. [EMBL/ GenBank/ DDBJ] [CoDingSequence] AC009488; AAP22357.1; -; Genomic_DNA. [EMBL/ GenBank/ DDBJ] [CoDingSequence] BC093628; AAH93628.1; -; mRNA. [EMBL/ GenBank/ DDBJ] [CoDingSequence] S65458; AAD13964.1; -; mRNA. [EMBL/ GenBank/ DDBJ] [CoDingSequence] PIR A01855; ZUHU.   PDB 1BUY; NMR; A=28-193. [ExPASy/RCSB/EBI] 1CN4; X-ray; C=28-193. [ExPASy/RCSB/EBI] 1EER; X-ray; A=28-193. [ExPASy/RCSB/EBI] GlycoSuiteDB P01588; -.   Ensembl ENSG00000130427; Homo sapiens. [Entry/Contig] HGNC HGNC:3415; EPO.   MIM 133170; gene. [MIM/EBI] GO Cellular component extracellular space GO:0005615 traceable author statement Biological process circulation GO:0008015 non-traceable author statement Biological process response to stress GO:0006950 traceable author statement Biological process signal transduction GO:0007165 non-traceable author statement [QuickGO] InterPro IPR009079; 4_helix_cytokine.   IPR012351; Cytokine_4_hlx.   IPR001323; EPO_TPO.   IPR003013; Erythroptn.   Graphical view of the domain structure   PANTHER PTHR10370; Erythroptn; 1.   Pfam PF00758; EPO_TPO; 1.   Pfam graphical view of domain structure   PIRSF PIRSF001951; EPO; 1.   PRINTS PR00272; ERYTHROPTN.   PROSITE PS00817; EPO_TPO; 1.   Keywords   3D-structure   Direct protein sequencing   Erythrocyte maturation   Glycoprotein   Hormone   Pharmaceutical   Polymorphism   Signal Features   Type From    To  Length Description Feature ID   SIGNAL  1     27      27       CHAIN  28    193     166 Erythropoietin PRO_0000008401   PROPEP  190    193       4 Removed in mature form (Probable) PRO_0000008402   CARBOHYD  51     51    N-linked (GlcNAc...) CAR_000052   CARBOHYD  65     65    N-linked (GlcNAc...) CAR_000166   CARBOHYD  110    110    N-linked (GlcNAc...) CAR_000192   CARBOHYD  153    153    O-linked (GalNAc...).     DISULFID  34    188          DISULFID  56     60          VARIANT  131    132    SL -> NF (in an hepatocellular carcinoma) VAR_009870   VARIANT  149    149    P -> Q (in an hepatocellular carcinoma) VAR_009871   CONFLICT  40     40    E -> Q (in Ref. 1; CAA26095).     CONFLICT  85     85    Q -> QQ (in Ref. 7).     CONFLICT  140    140    G -> R (in Ref. 1; CAA26095).     STRAND  31     31       1       HELIX  32     34       3       HELIX  141    147       7       TURN  148    149       2       STRAND  151    151       1       STRAND  160    164       5       HELIX  165    177      13       TURN  178    178       1       HELIX  179    188      10       Sequence information Length 193 AA Molecular weight 21307 Da CRC64 C91F0E4C26A52033    [This is a checksum on the sequence] MGVHECPAWL WLLLSLLSLP LGLPVLGAPP RLICDSRVLE RYLLEAKEAE  50 NITTGCAEHC SLNENITVPD TKVNFYAWKR MEVGQQAVEV WQGLALLSEA 100 VLRGQALLVN SSQPWEPLQL HVDKAVSGLR SLTTLLRALG AQKEAISPPD 150 AASAAPLRTI TADTFRKLFR VYSNFLRGKL KLYTGEACRT GDR        193

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