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P04279

- SEMG1_HUMAN

UniProt

P04279 - SEMG1_HUMAN

Protein

Semenogelin-1

Gene

SEMG1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 2 (01 Jan 1990)
      Previous versions | rss
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    Functioni

    Predominant protein in semen. It participates in the formation of a gel matrix entrapping the accessory gland secretions and ejaculated spermatozoa. Fragments of semenogelin and/or fragments of the related proteins may contribute to the activation of progressive sperm movements as the gel-forming proteins are fragmented by KLK3/PSA.1 Publication
    Alpha-inhibin-92 and alpha-inhibin-31, derived from the proteolytic degradation of semenogelin, inhibit the secretion of pituitary follicle-stimulating hormone.1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. structural molecule activity Source: InterPro

    GO - Biological processi

    1. insemination Source: ProtInc

    Enzyme and pathway databases

    ReactomeiREACT_75925. Amyloids.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Semenogelin-1
    Alternative name(s):
    Semenogelin I
    Short name:
    SGI
    Cleaved into the following 3 chains:
    Gene namesi
    Name:SEMG1
    Synonyms:SEMG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:10742. SEMG1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: ProtInc
    3. nucleus Source: UniProt
    4. secretory granule Source: InterPro

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi239 – 2391C → G: Abrogates binding to EPPIN and do not inhibit spem motility. 1 Publication

    Organism-specific databases

    PharmGKBiPA35664.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Add
    BLAST
    Chaini24 – 462439Semenogelin-1PRO_0000032351Add
    BLAST
    Peptidei68 – 15992Alpha-inhibin-92PRO_0000032352Add
    BLAST
    Peptidei108 – 15952Seminal basic proteinPRO_0000032353Add
    BLAST
    Peptidei108 – 13831Alpha-inhibin-31PRO_0000032354Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei24 – 241Pyrrolidone carboxylic acidCurated
    Disulfide bondi239 – 239Interchain

    Post-translational modificationi

    Transglutaminase substrate.
    Rapidly cleaved after ejaculation by KLK3/PSA, resulting in liquefaction of the semen coagulum and the progressive release of motile spermatozoa.

    Keywords - PTMi

    Disulfide bond, Pyrrolidone carboxylic acid

    Proteomic databases

    MaxQBiP04279.
    PaxDbiP04279.
    PRIDEiP04279.

    PTM databases

    PhosphoSiteiP04279.

    Miscellaneous databases

    PMAP-CutDBP04279.

    Expressioni

    Tissue specificityi

    Seminal vesicle.

    Gene expression databases

    ArrayExpressiP04279.
    BgeeiP04279.
    CleanExiHS_SEMG1.
    GenevestigatoriP04279.

    Organism-specific databases

    HPAiHPA042476.

    Interactioni

    Subunit structurei

    Occurs in disulfide-linked complexes which may also contain two less abundant 71- and 76-kDa semenogelin-related polypeptides. Interacts with EPPIN (via C-terminus); Cys-239 is a critical amino acid for both binding to EPPIN.2 Publications

    Protein-protein interaction databases

    BioGridi112306. 7 interactions.
    IntActiP04279. 2 interactions.
    MINTiMINT-2862979.

    Structurei

    3D structure databases

    ProteinModelPortaliP04279.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati70 – 129603-1Add
    BLAST
    Repeati141 – 200602-1Add
    BLAST
    Repeati201 – 260602-2Add
    BLAST
    Repeati381 – 439593-2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni70 – 439370Repeat-rich regionBy similarityAdd
    BLAST
    Regioni164 – 283120Interaction with EPPINAdd
    BLAST
    Regioni261 – 3801202 X 60 AA tandem repeats, type 1Add
    BLAST

    Sequence similaritiesi

    Belongs to the semenogelin family.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG74001.
    HOVERGENiHBG054194.
    InParanoidiP04279.
    OMAiQNPNQDQ.
    OrthoDBiEOG7J4469.
    PhylomeDBiP04279.
    TreeFamiTF342360.

    Family and domain databases

    InterProiIPR008836. Semenogelin.
    [Graphical view]
    PANTHERiPTHR10547. PTHR10547. 1 hit.
    PfamiPF05474. Semenogelin. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P04279-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MKPNIIFVLS LLLILEKQAA VMGQKGGSKG RLPSEFSQFP HGQKGQHYSG    50
    QKGKQQTESK GSFSIQYTYH VDANDHDQSR KSQQYDLNAL HKTTKSQRHL 100
    GGSQQLLHNK QEGRDHDKSK GHFHRVVIHH KGGKAHRGTQ NPSQDQGNSP 150
    SGKGISSQYS NTEERLWVHG LSKEQTSVSG AQKGRKQGGS QSSYVLQTEE 200
    LVANKQQRET KNSHQNKGHY QNVVEVREEH SSKVQTSLCP AHQDKLQHGS 250
    KDIFSTQDEL LVYNKNQHQT KNLNQDQQHG RKANKISYQS SSTEERRLHY 300
    GENGVQKDVS QSSIYSQTEE KAQGKSQKQI TIPSQEQEHS QKANKISYQS 350
    SSTEERRLHY GENGVQKDVS QRSIYSQTEK LVAGKSQIQA PNPKQEPWHG 400
    ENAKGESGQS TNREQDLLSH EQKGRHQHGS HGGLDIVIIE QEDDSDRHLA 450
    QHLNNDRNPL FT 462
    Length:462
    Mass (Da):52,131
    Last modified:January 1, 1990 - v2
    Checksum:i760F48EFCF2FA702
    GO
    Isoform 2 (identifier: P04279-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         312-371: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:402
    Mass (Da):45,322
    Checksum:i4D7F264E7C7FC15D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti100 – 1001L → Q in AAP82463. (PubMed:14629036)Curated
    Sequence conflicti235 – 2373QTS → LRT in AAO20112. (PubMed:14562960)Curated
    Sequence conflicti235 – 2373QTS → LRT in AAO20113. (PubMed:14562960)Curated
    Sequence conflicti321 – 3211K → L AA sequence (PubMed:2757795)Curated
    Sequence conflicti423 – 4231K → N in CAA87636. (PubMed:1517240)Curated
    Sequence conflicti423 – 4231K → N in AAA18168. (PubMed:1517240)Curated
    Sequence conflicti457 – 4571R → Q1 PublicationCurated
    Sequence conflicti457 – 4571R → Q(PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti58 – 581E → G.
    Corresponds to variant rs11559137 [ dbSNP | Ensembl ].
    VAR_053650
    Natural varianti79 – 791S → T Less common genetic variant. 2 Publications
    Corresponds to variant rs2301366 [ dbSNP | Ensembl ].
    VAR_005610
    Natural varianti108 – 1081H → R.
    Corresponds to variant rs2233884 [ dbSNP | Ensembl ].
    VAR_053651
    Natural varianti372 – 3721R → L.1 Publication
    Corresponds to variant rs2233887 [ dbSNP | Ensembl ].
    VAR_022679

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei312 – 37160Missing in isoform 2. 2 PublicationsVSP_004385Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04440 mRNA. Translation: AAB59506.1.
    Z47556 Genomic DNA. Translation: CAA87636.1.
    M81650 Genomic DNA. Translation: AAA18168.1.
    AY256465 Genomic DNA. Translation: AAP82462.1.
    AY256466 Genomic DNA. Translation: AAP82463.1.
    AY256467 Genomic DNA. Translation: AAP82464.1.
    AY256468 Genomic DNA. Translation: AAP82465.1.
    AY256469 Genomic DNA. Translation: AAP82466.1.
    BT007177 mRNA. Translation: AAP35841.1.
    AL049767 Genomic DNA. Translation: CAB53523.1.
    CH471077 Genomic DNA. Translation: EAW75871.1.
    BC007096 mRNA. Translation: AAH07096.1.
    BC055416 mRNA. Translation: AAH55416.1.
    AY174423 Genomic DNA. Translation: AAO20112.1.
    AY174424 Genomic DNA. Translation: AAO20113.1.
    AY174437 Genomic DNA. Translation: AAO20126.1.
    CCDSiCCDS13345.1. [P04279-1]
    PIRiB43412. WTHUB.
    RefSeqiNP_002998.1. NM_003007.3. [P04279-1]
    UniGeneiHs.1968.

    Genome annotation databases

    EnsembliENST00000372781; ENSP00000361867; ENSG00000124233. [P04279-1]
    GeneIDi6406.
    KEGGihsa:6406.
    UCSCiuc002xni.2. human. [P04279-1]
    uc002xnj.2. human. [P04279-2]

    Polymorphism databases

    DMDMi134426.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    Shackled sperm - Issue 62 of September 2005

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04440 mRNA. Translation: AAB59506.1 .
    Z47556 Genomic DNA. Translation: CAA87636.1 .
    M81650 Genomic DNA. Translation: AAA18168.1 .
    AY256465 Genomic DNA. Translation: AAP82462.1 .
    AY256466 Genomic DNA. Translation: AAP82463.1 .
    AY256467 Genomic DNA. Translation: AAP82464.1 .
    AY256468 Genomic DNA. Translation: AAP82465.1 .
    AY256469 Genomic DNA. Translation: AAP82466.1 .
    BT007177 mRNA. Translation: AAP35841.1 .
    AL049767 Genomic DNA. Translation: CAB53523.1 .
    CH471077 Genomic DNA. Translation: EAW75871.1 .
    BC007096 mRNA. Translation: AAH07096.1 .
    BC055416 mRNA. Translation: AAH55416.1 .
    AY174423 Genomic DNA. Translation: AAO20112.1 .
    AY174424 Genomic DNA. Translation: AAO20113.1 .
    AY174437 Genomic DNA. Translation: AAO20126.1 .
    CCDSi CCDS13345.1. [P04279-1 ]
    PIRi B43412. WTHUB.
    RefSeqi NP_002998.1. NM_003007.3. [P04279-1 ]
    UniGenei Hs.1968.

    3D structure databases

    ProteinModelPortali P04279.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112306. 7 interactions.
    IntActi P04279. 2 interactions.
    MINTi MINT-2862979.

    PTM databases

    PhosphoSitei P04279.

    Polymorphism databases

    DMDMi 134426.

    Proteomic databases

    MaxQBi P04279.
    PaxDbi P04279.
    PRIDEi P04279.

    Protocols and materials databases

    DNASUi 6406.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000372781 ; ENSP00000361867 ; ENSG00000124233 . [P04279-1 ]
    GeneIDi 6406.
    KEGGi hsa:6406.
    UCSCi uc002xni.2. human. [P04279-1 ]
    uc002xnj.2. human. [P04279-2 ]

    Organism-specific databases

    CTDi 6406.
    GeneCardsi GC20P043835.
    HGNCi HGNC:10742. SEMG1.
    HPAi HPA042476.
    MIMi 182140. gene.
    neXtProti NX_P04279.
    PharmGKBi PA35664.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG74001.
    HOVERGENi HBG054194.
    InParanoidi P04279.
    OMAi QNPNQDQ.
    OrthoDBi EOG7J4469.
    PhylomeDBi P04279.
    TreeFami TF342360.

    Enzyme and pathway databases

    Reactomei REACT_75925. Amyloids.

    Miscellaneous databases

    GeneWikii Semenogelin_I.
    GenomeRNAii 6406.
    NextBioi 24890.
    PMAP-CutDB P04279.
    PROi P04279.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P04279.
    Bgeei P04279.
    CleanExi HS_SEMG1.
    Genevestigatori P04279.

    Family and domain databases

    InterProi IPR008836. Semenogelin.
    [Graphical view ]
    PANTHERi PTHR10547. PTHR10547. 1 hit.
    Pfami PF05474. Semenogelin. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Semenogelin, the predominant protein in human semen. Primary structure and identification of closely related proteins in the male accessory sex glands and on the spermatozoa."
      Lilja H., Abrahamsson P.-A., Lundwall A.
      J. Biol. Chem. 264:1894-1900(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Gene structure of semenogelin I and II. The predominant proteins in human semen are encoded by two homologous genes on chromosome 20."
      Ulvsbaeck M., Lazure C., Lilja H., Spurr N.K., Rao V.V., Loeffler C., Hansmann I., Lundwall A.
      J. Biol. Chem. 267:18080-18084(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Blood.
    3. "Evolution of the hominoid semenogelin genes, the major proteins of ejaculated semen."
      Jensen-Seaman M.I., Li W.-H.
      J. Mol. Evol. 57:261-270(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-79 AND LEU-372.
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    5. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [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] (ISOFORM 2).
      Tissue: Prostate.
    8. "Reduced polymorphism in the chimpanzee semen coagulating protein, semenogelin I."
      Kingan S.B., Tatar M., Rand D.M.
      J. Mol. Evol. 57:159-169(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 62-237 AND 241-449, VARIANT THR-79.
    9. "Amino acid sequence of the predominant basic protein in human seminal plasma."
      Lilja H., Jeppsson J.-O.
      FEBS Lett. 182:181-184(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 108-159.
    10. "Partial amino acid sequence of a human seminal plasma peptide with inhibin-like activity."
      Seidah N.G., Ramasharma K., Sairam M.R., Chretien M.
      FEBS Lett. 167:98-102(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 108-138.
    11. "Isolation, structure, and synthesis of a human seminal plasma peptide with inhibin-like activity."
      Ramasharma K., Sairam M.R., Seidah N.G., Chretien M., Manjunath P., Schiller P.W., Yamashiro D., Li C.H.
      Science 223:1199-1202(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 108-138.
    12. "Isolation and structure determination of two peptides occurring in human seminal plasma."
      Schneider K., Kausler W., Tripier D., Jouvenal K., Spiteller G.
      Biol. Chem. Hoppe-Seyler 370:353-356(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 316-344.
    13. "Isolation and identification of N-terminally extended forms of 5-oxoprolylglutamylprolinamide (Glp-Glu-Pro-NH2), a thyrotropin-releasing-hormone (TRH)-like peptide present in human semen."
      Khan Z., Smyth D.G.
      Eur. J. Biochem. 212:35-40(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 373-397.
    14. "Human seminal alpha inhibins: isolation, characterization, and structure."
      Li C.H., Hammonds R.G., Ramasharma K., Chung D.
      Proc. Natl. Acad. Sci. U.S.A. 82:4041-4044(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 68-159.
    15. "Semenogelin I: a coagulum forming, multifunctional seminal vesicle protein."
      Robert M., Gagnon C.
      Cell. Mol. Life Sci. 55:944-960(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    16. "Association of eppin with semenogelin on human spermatozoa."
      Wang Z., Widgren E.E., Sivashanmugam P., O'Rand M.G., Richardson R.T.
      Biol. Reprod. 72:1064-1070(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EPPIN.
    17. "Characterization of an eppin protein complex from human semen and spermatozoa."
      Wang Z., Widgren E.E., Richardson R.T., O'Rand M.G.
      Biol. Reprod. 77:476-484(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH LTF; CLU AND EPPIN.
    18. "Analysis of recombinant human semenogelin as an inhibitor of human sperm motility."
      Mitra A., Richardson R.T., O'Rand M.G.
      Biol. Reprod. 82:489-496(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-239.

    Entry informationi

    Entry nameiSEMG1_HUMAN
    AccessioniPrimary (citable) accession number: P04279
    Secondary accession number(s): Q53ZV0
    , Q53ZV1, Q53ZV2, Q6X4I9, Q6Y809, Q6Y822, Q6Y823, Q86U64, Q96QM3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 1987
    Last sequence update: January 1, 1990
    Last modified: October 1, 2014
    This is version 154 of the entry and version 2 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3