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Q9Y2G5

- OFUT2_HUMAN

UniProt

Q9Y2G5 - OFUT2_HUMAN

Protein

GDP-fucose protein O-fucosyltransferase 2

Gene

POFUT2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 3 (15 Feb 2005)
      Previous versions | rss
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    Functioni

    Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X(2,3)-S/T-C2-X(2)-G of thrombospondin type 1 repeats where C1 and C2 are the first and second cysteines, respectively. O-fucosylates members of several protein families including the ADAMTS family, the thrombosporin (TSP) and spondin families. The O-fucosylation of TSRs is also required for restricting epithelial to mesenchymal transition (EMT), maintaining the correct patterning of mesoderm and localization of the definite endoderm By similarity. Required for the proper secretion of ADAMTS family members such as ADAMSL1 and ADAMST13.By similarity5 Publications

    Catalytic activityi

    Transfers an alpha-L-fucosyl residue from GDP-beta-L-fucose to the serine hydroxy group of a protein acceptor.1 Publication

    Enzyme regulationi

    Inhibited by EDTA and by Zn2+.1 Publication

    Kineticsi

    1. KM=9.8 µM for GDP-fucose1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei54 – 541Proton donor/acceptorCurated
    Binding sitei294 – 2941Substrate
    Sitei396 – 3961Essential for catalytic activity

    GO - Molecular functioni

    1. peptide-O-fucosyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. fucose metabolic process Source: UniProtKB-KW
    2. mesoderm formation Source: Ensembl
    3. protein O-linked fucosylation Source: UniProtKB
    4. regulation of epithelial to mesenchymal transition Source: Ensembl
    5. regulation of gene expression Source: Ensembl
    6. regulation of secretion Source: UniProtKB

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Fucose metabolism

    Enzyme and pathway databases

    ReactomeiREACT_200626. O-glycosylation of TSR domain-containing proteins.
    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGT68. Glycosyltransferase Family 68.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GDP-fucose protein O-fucosyltransferase 2 (EC:2.4.1.221)
    Alternative name(s):
    Peptide-O-fucosyltransferase 2
    Short name:
    O-FucT-2
    Gene namesi
    Name:POFUT2
    Synonyms:C21orf80, FUT13, KIAA0958
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:14683. POFUT2.

    Subcellular locationi

    Endoplasmic reticulum 1 Publication. Golgi apparatus 1 Publication
    Note: Mainly located in the endoplasmic reticulum.

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB-SubCell
    2. Golgi apparatus Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Golgi apparatus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi54 – 541E → A: Abolishes enzyme activity. 1 Publication
    Mutagenesisi92 – 921W → A: Abolishes enzyme activity. 1 Publication
    Mutagenesisi152 – 1521W → A: Reduces enzyme activity. 1 Publication
    Mutagenesisi273 – 2731W → A: Reduces enzyme activity. 1 Publication
    Mutagenesisi294 – 2941R → A: Abolishes enzyme activity. 1 Publication
    Mutagenesisi297 – 2971D → A: Reduces enzyme activity. 1 Publication
    Mutagenesisi395 – 3951E → A: No enhanced secretion of ADASMTS13; when associated with A-396. 1 Publication
    Mutagenesisi396 – 3961E → A: Reduces enzyme activity. No enhanced secretion of ADASMTS13; when associated with A-396. 2 Publications

    Organism-specific databases

    PharmGKBiPA25867.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 429408GDP-fucose protein O-fucosyltransferase 2PRO_0000012154Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi161 ↔ 1921 Publication
    Glycosylationi189 – 1891N-linked (GlcNAc...)1 Publication
    Glycosylationi209 – 2091N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi259 – 2591N-linked (GlcNAc...)1 Publication
    Disulfide bondi412 ↔ 4191 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ9Y2G5.
    PaxDbiQ9Y2G5.
    PRIDEiQ9Y2G5.

    PTM databases

    PhosphoSiteiQ9Y2G5.

    Expressioni

    Tissue specificityi

    Isoform A is expressed in fetal liver and peripheral blood lymphocytes. Isoform B is expressed in spleen, lung, testis, bone marrow, thymus, pancreas, prostate, fetal brain, fetal liver and fetal kidney. Isoform C is expressed in brain, heart, spleen, liver, lung, stomach, testis, placenta, skin, thymus, pancreas, mammary gland, prostate, fetal brain, fetal liver and fetal heart.1 Publication

    Gene expression databases

    ArrayExpressiQ9Y2G5.
    BgeeiQ9Y2G5.
    CleanExiHS_POFUT2.
    GenevestigatoriQ9Y2G5.

    Organism-specific databases

    HPAiHPA044297.

    Interactioni

    Protein-protein interaction databases

    BioGridi116876. 2 interactions.
    IntActiQ9Y2G5. 3 interactions.
    STRINGi9606.ENSP00000339613.

    Structurei

    Secondary structure

    1
    429
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi44 – 485
    Helixi56 – 7419
    Beta strandi79 – 835
    Helixi91 – 933
    Helixi104 – 1063
    Helixi110 – 1145
    Beta strandi119 – 1213
    Helixi122 – 1287
    Beta strandi129 – 14113
    Beta strandi156 – 1594
    Helixi179 – 1813
    Beta strandi186 – 19510
    Helixi199 – 2024
    Helixi203 – 2086
    Beta strandi213 – 2197
    Helixi220 – 2223
    Helixi231 – 2388
    Helixi244 – 25815
    Turni262 – 2665
    Helixi273 – 2753
    Beta strandi286 – 2938
    Turni296 – 3027
    Beta strandi304 – 3063
    Helixi309 – 32315
    Beta strandi328 – 3325
    Helixi336 – 34510
    Beta strandi349 – 3513
    Helixi356 – 37621
    Beta strandi378 – 3836
    Helixi388 – 40013
    Helixi404 – 4063

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4AP5X-ray3.00A/B22-429[»]
    4AP6X-ray3.40A/B/C/D37-429[»]
    ProteinModelPortaliQ9Y2G5.
    SMRiQ9Y2G5. Positions 41-429.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni53 – 564Substrate binding
    Regioni388 – 3892Substrate binding

    Sequence similaritiesi

    Belongs to the glycosyltransferase 68 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG77810.
    HOVERGENiHBG053367.
    InParanoidiQ9Y2G5.
    KOiK03691.
    OMAiICAHARC.
    OrthoDBiEOG76T9S1.
    PhylomeDBiQ9Y2G5.
    TreeFamiTF314337.

    Family and domain databases

    InterProiIPR019378. GDP-Fuc_O-FucTrfase.
    [Graphical view]
    PfamiPF10250. O-FucT. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform C (identifier: Q9Y2G5-3) [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

    MATLSFVFLL LGAVSWPPAS ASGQEFWPGQ SAADILSGAA SRRRYLLYDV    50
    NPPEGFNLRR DVYIRIASLL KTLLKTEEWV LVLPPWGRLY HWQSPDIHQV 100
    RIPWSEFFDL PSLNKNIPVI EYEQFIAESG GPFIDQVYVL QSYAEGWKEG 150
    TWEEKVDERP CIDQLLYSQD KHEYYRGWFW GYEETRGLNV SCLSVQGSAS 200
    IVAPLLLRNT SARSVMLDRA ENLLHDHYGG KEYWDTRRSM VFARHLREVG 250
    DEFRSRHLNS TDDADRIPFQ EDWMKMKVKL GSALGGPYLG VHLRRKDFIW 300
    GHRQDVPSLE GAVRKIRSLM KTHRLDKVFV ATDAVRKEYE ELKKLLPEMV 350
    RFEPTWEELE LYKDGGVAII DQWICAHARF FIGTSVSTFS FRIHEEREIL 400
    GLDPKTTYNR FCGDQEKACE QPTHWKITY 429
    Length:429
    Mass (Da):49,976
    Last modified:February 15, 2005 - v3
    Checksum:i36A4213D905AFFD1
    GO
    Isoform A (identifier: Q9Y2G5-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         380-429: FFIGTSVSTF...EQPTHWKITY → CLPTSLSAES...GHFHTVCLLV

    Show »
    Length:424
    Mass (Da):48,896
    Checksum:i60BA687F0DFB8875
    GO
    Isoform B (identifier: Q9Y2G5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         379-380: RF → SS
         381-429: Missing.

    Show »
    Length:380
    Mass (Da):44,083
    Checksum:i7D640225C9A977C0
    GO

    Sequence cautioni

    The sequence BAA76802.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAB90496.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei379 – 3802RF → SS in isoform B. 3 PublicationsVSP_003833
    Alternative sequencei380 – 42950FFIGT…WKITY → CLPTSLSAESGSGGFQRFFC PKYSVSEQMVACVHSGHFHT VCLLV in isoform A. 2 PublicationsVSP_003832Add
    BLAST
    Alternative sequencei381 – 42949Missing in isoform B. 3 PublicationsVSP_003834Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ302080 mRNA. Translation: CAC24557.1.
    AJ302079 mRNA. Translation: CAC24556.1.
    AY066015 mRNA. Translation: AAL47681.2.
    AJ575591 mRNA. Translation: CAE01472.1.
    AB023175 mRNA. Translation: BAA76802.1. Different initiation.
    AL110285 mRNA. Translation: CAB53715.2.
    AL163301 Genomic DNA. Translation: CAB90496.1. Different initiation.
    BC011044 mRNA. Translation: AAH11044.1.
    BC064623 mRNA. Translation: AAH64623.1.
    CCDSiCCDS13719.1. [Q9Y2G5-3]
    CCDS13721.1. [Q9Y2G5-1]
    RefSeqiNP_056042.1. NM_015227.4. [Q9Y2G5-1]
    NP_598368.2. NM_133635.4. [Q9Y2G5-3]
    UniGeneiHs.592164.

    Genome annotation databases

    EnsembliENST00000331343; ENSP00000329682; ENSG00000186866. [Q9Y2G5-1]
    ENST00000334538; ENSP00000335427; ENSG00000186866. [Q9Y2G5-2]
    ENST00000349485; ENSP00000339613; ENSG00000186866. [Q9Y2G5-3]
    GeneIDi23275.
    KEGGihsa:23275.
    UCSCiuc002zhc.3. human. [Q9Y2G5-3]
    uc002zhd.3. human. [Q9Y2G5-1]

    Polymorphism databases

    DMDMi59803123.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Functional Glycomics Gateway - GTase

    Peptide-O-fucosyltransferase 2

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ302080 mRNA. Translation: CAC24557.1 .
    AJ302079 mRNA. Translation: CAC24556.1 .
    AY066015 mRNA. Translation: AAL47681.2 .
    AJ575591 mRNA. Translation: CAE01472.1 .
    AB023175 mRNA. Translation: BAA76802.1 . Different initiation.
    AL110285 mRNA. Translation: CAB53715.2 .
    AL163301 Genomic DNA. Translation: CAB90496.1 . Different initiation.
    BC011044 mRNA. Translation: AAH11044.1 .
    BC064623 mRNA. Translation: AAH64623.1 .
    CCDSi CCDS13719.1. [Q9Y2G5-3 ]
    CCDS13721.1. [Q9Y2G5-1 ]
    RefSeqi NP_056042.1. NM_015227.4. [Q9Y2G5-1 ]
    NP_598368.2. NM_133635.4. [Q9Y2G5-3 ]
    UniGenei Hs.592164.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4AP5 X-ray 3.00 A/B 22-429 [» ]
    4AP6 X-ray 3.40 A/B/C/D 37-429 [» ]
    ProteinModelPortali Q9Y2G5.
    SMRi Q9Y2G5. Positions 41-429.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116876. 2 interactions.
    IntActi Q9Y2G5. 3 interactions.
    STRINGi 9606.ENSP00000339613.

    Protein family/group databases

    CAZyi GT68. Glycosyltransferase Family 68.

    PTM databases

    PhosphoSitei Q9Y2G5.

    Polymorphism databases

    DMDMi 59803123.

    Proteomic databases

    MaxQBi Q9Y2G5.
    PaxDbi Q9Y2G5.
    PRIDEi Q9Y2G5.

    Protocols and materials databases

    DNASUi 23275.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000331343 ; ENSP00000329682 ; ENSG00000186866 . [Q9Y2G5-1 ]
    ENST00000334538 ; ENSP00000335427 ; ENSG00000186866 . [Q9Y2G5-2 ]
    ENST00000349485 ; ENSP00000339613 ; ENSG00000186866 . [Q9Y2G5-3 ]
    GeneIDi 23275.
    KEGGi hsa:23275.
    UCSCi uc002zhc.3. human. [Q9Y2G5-3 ]
    uc002zhd.3. human. [Q9Y2G5-1 ]

    Organism-specific databases

    CTDi 23275.
    GeneCardsi GC21M046683.
    HGNCi HGNC:14683. POFUT2.
    HPAi HPA044297.
    MIMi 610249. gene.
    neXtProti NX_Q9Y2G5.
    PharmGKBi PA25867.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG77810.
    HOVERGENi HBG053367.
    InParanoidi Q9Y2G5.
    KOi K03691.
    OMAi ICAHARC.
    OrthoDBi EOG76T9S1.
    PhylomeDBi Q9Y2G5.
    TreeFami TF314337.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    Reactomei REACT_200626. O-glycosylation of TSR domain-containing proteins.

    Miscellaneous databases

    GenomeRNAii 23275.
    NextBioi 45054.
    PROi Q9Y2G5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y2G5.
    Bgeei Q9Y2G5.
    CleanExi HS_POFUT2.
    Genevestigatori Q9Y2G5.

    Family and domain databases

    InterProi IPR019378. GDP-Fuc_O-FucTrfase.
    [Graphical view ]
    Pfami PF10250. O-FucT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Caenorhabditis elegans ortholog of C21orf80, a potential new protein O-fucosyltransferase, is required for normal development."
      Menzel O., Vellai T., Takacs-Vellai K., Reymond A., Mueller F., Antonarakis S.E., Guipponi M.
      Genomics 84:320-330(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. "A new superfamily of protein-O-fucosyltransferases, alpha2-fucosyltransferases, and alpha6-fucosyltransferases: phylogeny and identification of conserved peptide motifs."
      Martinez-Duncker I., Mollicone R., Candelier J.-J., Breton C., Oriol R.
      Glycobiology 13:1C-5C(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
    3. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
      Tissue: Brain.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
      Tissue: Testis.
    5. "The DNA sequence of human chromosome 21."
      Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
      , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
      Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORMS B AND C).
      Tissue: Brain.
    7. "C-mannosylation and O-fucosylation of the thrombospondin type 1 module."
      Hofsteenge J., Huwiler K.G., Macek B., Hess D., Lawler J., Mosher D.F., Peter-Katalinic J.
      J. Biol. Chem. 276:6485-6498(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Two distinct pathways for O-fucosylation of epidermal growth factor-like or thrombospondin type 1 repeats."
      Luo Y., Nita-Lazar A., Haltiwanger R.S.
      J. Biol. Chem. 281:9385-9392(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. Cited for: FUNCTION, MUTAGENESIS OF GLU-395 AND GLU-396.
    10. "O-fucosylation of thrombospondin type 1 repeats in ADAMTS-like-1/punctin-1 regulates secretion: implications for the ADAMTS superfamily."
      Wang L.W., Dlugosz M., Somerville R.P., Raed M., Haltiwanger R.S., Apte S.S.
      J. Biol. Chem. 282:17024-17031(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Structure of human POFUT2: insights into thrombospondin type 1 repeat fold and O-fucosylation."
      Chen C.I., Keusch J.J., Klein D., Hess D., Hofsteenge J., Gut H.
      EMBO J. 31:3183-3197(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 22-429 IN COMPLEX WITH GDP-FUCOSE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLU-54; TRP-92; TRP-152; TRP-273; ARG-294; ASP-297 AND GLU-396, GLYCOSYLATION AT ASN-189 AND ASN-259, DISULFIDE BONDS.

    Entry informationi

    Entry nameiOFUT2_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y2G5
    Secondary accession number(s): Q6PJV1
    , Q7Z4N0, Q8WWU6, Q9BQS4, Q9BQS5, Q9UFY3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: February 15, 2005
    Last modified: October 1, 2014
    This is version 107 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 21
      Human chromosome 21: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3