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Protein

GDP-fucose protein O-fucosyltransferase 2

Gene

POFUT2

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

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

    Pathway: protein glycosylation

    This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
    View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

    Sites

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

    GO - Molecular functioni

    • peptide-O-fucosyltransferase activity Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Fucose metabolism

    Enzyme and pathway databases

    BRENDAi2.4.1.221. 2681.
    ReactomeiREACT_264269. 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 Componenti: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:14683. POFUT2.

    Subcellular locationi

    GO - Cellular componenti

    • endoplasmic reticulum membrane Source: Reactome
    • Golgi apparatus Source: UniProtKB
    Complete GO annotation...

    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.

    Polymorphism and mutation databases

    BioMutaiPOFUT2.
    DMDMi59803123.

    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

    BgeeiQ9Y2G5.
    CleanExiHS_POFUT2.
    ExpressionAtlasiQ9Y2G5. baseline and differential.
    GenevisibleiQ9Y2G5. HS.

    Organism-specific databases

    HPAiHPA044297.

    Interactioni

    Protein-protein interaction databases

    BioGridi116876. 1 interaction.
    IntActiQ9Y2G5. 3 interactions.
    STRINGi9606.ENSP00000339613.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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.
    GeneTreeiENSGT00390000007989.
    HOVERGENiHBG053367.
    InParanoidiQ9Y2G5.
    KOiK03691.
    OMAiICAHARF.
    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. AlignAdd to basket

    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

            10         20         30         40         50
    MATLSFVFLL LGAVSWPPAS ASGQEFWPGQ SAADILSGAA SRRRYLLYDV
    60 70 80 90 100
    NPPEGFNLRR DVYIRIASLL KTLLKTEEWV LVLPPWGRLY HWQSPDIHQV
    110 120 130 140 150
    RIPWSEFFDL PSLNKNIPVI EYEQFIAESG GPFIDQVYVL QSYAEGWKEG
    160 170 180 190 200
    TWEEKVDERP CIDQLLYSQD KHEYYRGWFW GYEETRGLNV SCLSVQGSAS
    210 220 230 240 250
    IVAPLLLRNT SARSVMLDRA ENLLHDHYGG KEYWDTRRSM VFARHLREVG
    260 270 280 290 300
    DEFRSRHLNS TDDADRIPFQ EDWMKMKVKL GSALGGPYLG VHLRRKDFIW
    310 320 330 340 350
    GHRQDVPSLE GAVRKIRSLM KTHRLDKVFV ATDAVRKEYE ELKKLLPEMV
    360 370 380 390 400
    RFEPTWEELE LYKDGGVAII DQWICAHARF FIGTSVSTFS FRIHEEREIL
    410 420
    GLDPKTTYNR FCGDQEKACE QPTHWKITY
    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.Curated
    The sequence CAB90496.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    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:
    EMBLi
    GenBanki
    DDBJi
    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]

    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:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

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

    Protein-protein interaction databases

    BioGridi116876. 1 interaction.
    IntActiQ9Y2G5. 3 interactions.
    STRINGi9606.ENSP00000339613.

    Protein family/group databases

    CAZyiGT68. Glycosyltransferase Family 68.

    PTM databases

    PhosphoSiteiQ9Y2G5.

    Polymorphism and mutation databases

    BioMutaiPOFUT2.
    DMDMi59803123.

    Proteomic databases

    MaxQBiQ9Y2G5.
    PaxDbiQ9Y2G5.
    PRIDEiQ9Y2G5.

    Protocols and materials databases

    DNASUi23275.
    Structural Biology KnowledgebaseSearch...

    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]

    Organism-specific databases

    CTDi23275.
    GeneCardsiGC21M046683.
    HGNCiHGNC:14683. POFUT2.
    HPAiHPA044297.
    MIMi610249. gene.
    neXtProtiNX_Q9Y2G5.
    PharmGKBiPA25867.
    HUGEiSearch...
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiNOG77810.
    GeneTreeiENSGT00390000007989.
    HOVERGENiHBG053367.
    InParanoidiQ9Y2G5.
    KOiK03691.
    OMAiICAHARF.
    OrthoDBiEOG76T9S1.
    PhylomeDBiQ9Y2G5.
    TreeFamiTF314337.

    Enzyme and pathway databases

    UniPathwayiUPA00378.
    BRENDAi2.4.1.221. 2681.
    ReactomeiREACT_264269. O-glycosylation of TSR domain-containing proteins.

    Miscellaneous databases

    GenomeRNAii23275.
    NextBioi45054.
    PROiQ9Y2G5.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9Y2G5.
    CleanExiHS_POFUT2.
    ExpressionAtlasiQ9Y2G5. baseline and differential.
    GenevisibleiQ9Y2G5. HS.

    Family and domain databases

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

    Publicationsi

    « Hide 'large scale' publications
    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: June 24, 2015
    This is version 114 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

    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.