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Q9Y4C5

- CHST2_HUMAN

UniProt

Q9Y4C5 - CHST2_HUMAN

Protein

Carbohydrate sulfotransferase 2

Gene

CHST2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 2 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues within keratan-like structures on N-linked glycans and within mucin-associated glycans that can ultimately serve as SELL ligands. SELL ligands are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation. Participates in biosynthesis of the SELL ligand sialyl 6-sulfo Lewis X and in lymphocyte homing to Peyer patches. Has no activity toward O-linked sugars. Its substrate specificity may be influenced by its subcellular location. Sulfates GlcNAc residues at terminal, non-reducing ends of oligosaccharide chains.1 Publication

    Kineticsi

    1. KM=3.9 µM for PAPS1 Publication
    2. KM=1.4 mM for BetaBnO-GlcNAc1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei152 – 1521Not glycosylated

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi173 – 1797PAPSCurated
    Nucleotide bindingi332 – 3409PAPSCurated

    GO - Molecular functioni

    1. N-acetylglucosamine 6-O-sulfotransferase activity Source: UniProtKB
    2. sulfotransferase activity Source: ProtInc

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. glycosaminoglycan metabolic process Source: Reactome
    3. inflammatory response Source: ProtInc
    4. keratan sulfate biosynthetic process Source: Reactome
    5. keratan sulfate metabolic process Source: Reactome
    6. multicellular organismal development Source: ProtInc
    7. N-acetylglucosamine metabolic process Source: UniProtKB
    8. small molecule metabolic process Source: Reactome
    9. sulfur compound metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Inflammatory response

    Enzyme and pathway databases

    ReactomeiREACT_121120. Keratan sulfate biosynthesis.
    SABIO-RKQ9Y4C5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbohydrate sulfotransferase 2 (EC:2.8.2.-)
    Alternative name(s):
    Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 2
    Short name:
    GST-2
    N-acetylglucosamine 6-O-sulfotransferase 1
    Short name:
    GlcNAc6ST-1
    Short name:
    Gn6ST-1
    Gene namesi
    Name:CHST2
    Synonyms:GN6ST
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:1970. CHST2.

    Subcellular locationi

    Golgi apparatustrans-Golgi network membrane 2 Publications; Single-pass type II membrane protein 2 Publications

    GO - Cellular componenti

    1. Golgi membrane Source: Reactome
    2. integral component of membrane Source: UniProtKB-KW
    3. intrinsic component of Golgi membrane Source: UniProtKB
    4. trans-Golgi network Source: UniProtKB

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi59 – 591C → S: Does not affect homodimerization. Abolishes homodimerization but not enzyme activity; when associated with S-39. 1 Publication
    Mutagenesisi86 – 861C → S: Induces migration in both homodimeric and monomeric forms. Abolishes homodimerization but not enzyme activity; when associated with S-12. 1 Publication
    Mutagenesisi174 – 1741R → A: Induces a strong decrease in enzyme activity. 1 Publication
    Mutagenesisi296 – 2961R → A: Induces a strong decrease in enzyme activity. 1 Publication
    Mutagenesisi304 – 3041K → A: Loss of function. 1 Publication
    Mutagenesisi332 – 3321R → A: Loss of function. 1 Publication
    Mutagenesisi341 – 3411R → A: Induces a strong decrease in enzyme activity. 1 Publication
    Mutagenesisi457 – 4571N → A: Reduced localization in the Golgi. 1 Publication
    Mutagenesisi475 – 4751N → A: Unable to sulfate the sialyl Lewis X tetrasaccharide. 1 Publication
    Mutagenesisi518 – 5181K → A: Has weak or no effect. 1 Publication
    Mutagenesisi519 – 5191D → A: Has weak or no effect. 1 Publication
    Mutagenesisi520 – 5201L → A: Has weak or no effect. 1 Publication
    Mutagenesisi521 – 5211S → A: No effect. 1 Publication
    Mutagenesisi522 – 5221K → A: No effect. 1 Publication
    Mutagenesisi523 – 5231T → A: Has weak or no effect. 1 Publication
    Mutagenesisi524 – 5241L → A or T: Induces a strong decrease in enzyme activity. 1 Publication
    Mutagenesisi525 – 5251L → A: Induces a strong decrease in enzyme activity. 1 Publication
    Mutagenesisi525 – 5251L → T: Has weak or no effect. 1 Publication
    Mutagenesisi526 – 5261R → A: Has weak or no effect. 1 Publication
    Mutagenesisi527 – 5271K → A: No effect. 1 Publication
    Mutagenesisi528 – 5281P → A: Has weak or no effect. 1 Publication
    Mutagenesisi529 – 5291R → A: No effect. 1 Publication
    Mutagenesisi530 – 5301L → A or T: Induces a strong decrease in enzyme activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA26502.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 530530Carbohydrate sulfotransferase 2PRO_0000085186Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi243 – 2431N-linked (GlcNAc...)1 Publication
    Glycosylationi457 – 4571N-linked (GlcNAc...)1 Publication
    Glycosylationi475 – 4751N-linked (GlcNAc...)1 Publication

    Post-translational modificationi

    Glycosylation at Asn-475 is required for catalytic activity.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9Y4C5.
    PRIDEiQ9Y4C5.

    PTM databases

    PhosphoSiteiQ9Y4C5.

    Expressioni

    Tissue specificityi

    Widely expressed. Highly expressed in bone marrow, peripheral blood leukocytes, spleen, brain, spinal cord, ovary and placenta. Expressed by high endothelial cells (HEVs) and leukocytes.3 Publications

    Inductioni

    Up-regulated upon cytokine activation.1 Publication

    Gene expression databases

    BgeeiQ9Y4C5.
    CleanExiHS_CHST2.
    GenevestigatoriQ9Y4C5.

    Organism-specific databases

    HPAiHPA013313.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. Homodimerization is not essential for enzyme activity.2 Publications

    Protein-protein interaction databases

    STRINGi9606.ENSP00000307911.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y4C5.
    SMRiQ9Y4C5. Positions 417-501.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 5454CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini76 – 530455LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei55 – 7521Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG67451.
    HOGENOMiHOG000261614.
    HOVERGENiHBG050949.
    InParanoidiQ9Y4C5.
    KOiK04745.
    OMAiMGGPADY.
    OrthoDBiEOG7RZ5S0.
    PhylomeDBiQ9Y4C5.
    TreeFamiTF342871.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR016469. Carbohydrate_sulfotransferase.
    IPR027417. P-loop_NTPase.
    IPR000863. Sulfotransferase_dom.
    [Graphical view]
    PfamiPF00685. Sulfotransfer_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005883. Carbohydrate_sulfotransferase. 1 hit.
    SUPFAMiSSF52540. SSF52540. 3 hits.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative initiation. Align

    Isoform 1 (identifier: Q9Y4C5-1) [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

    MSRSPQRALP PGALPRLLQA APAAAPRALL PQWPRRPGRR WPASPLGMKV    50
    FRRKALVLCA GYALLLVLTM LNLLDYKWHK EPLQQCNPDG PLGAAAGAAG 100
    GSWGRPGPPP AGPPRAHARL DLRTPYRPPA AAVGAAPAAA AGMAGVAAPP 150
    GNGTRGTGGV GDKRQLVYVF TTWRSGSSFF GELFNQNPEV FFLYEPVWHV 200
    WQKLYPGDAV SLQGAARDML SALYRCDLSV FQLYSPAGSG GRNLTTLGIF 250
    GAATNKVVCS SPLCPAYRKE VVGLVDDRVC KKCPPQRLAR FEEECRKYRT 300
    LVIKGVRVFD VAVLAPLLRD PALDLKVIHL VRDPRAVASS RIRSRHGLIR 350
    ESLQVVRSRD PRAHRMPFLE AAGHKLGAKK EGVGGPADYH ALGAMEVICN 400
    SMAKTLQTAL QPPDWLQGHY LVVRYEDLVG DPVKTLRRVY DFVGLLVSPE 450
    MEQFALNMTS GSGSSSKPFV VSARNATQAA NAWRTALTFQ QIKQVEEFCY 500
    QPMAVLGYER VNSPEEVKDL SKTLLRKPRL 530
    Length:530
    Mass (Da):57,857
    Last modified:March 1, 2003 - v2
    Checksum:iA82CA227B9D5651B
    GO
    Isoform 2 (identifier: Q9Y4C5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-47: Missing.

    Note: Higher levels of expression compared to isoform 1 when expressed in HeLa cells. Exhibits similar intracellular GlcNAc-6-O-sulfation activity.

    Show »
    Length:483
    Mass (Da):52,787
    Checksum:iE27797D44931BA18
    GO

    Sequence cautioni

    The sequence BAA34265.2 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB16886.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB16887.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81A → V in BAB16887. (PubMed:11042394)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4747Missing in isoform 2. CuratedVSP_018887Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB014679 mRNA. Translation: BAA34265.2. Different initiation.
    AB014680 mRNA. Translation: BAA34266.2.
    AF083066 mRNA. Translation: AAD20981.1.
    AB021124 mRNA. Translation: BAB16886.1. Different initiation.
    AB021125 Genomic DNA. Translation: BAB16887.1. Different initiation.
    CH471052 Genomic DNA. Translation: EAW78952.1.
    CH471052 Genomic DNA. Translation: EAW78953.1.
    BC105010 mRNA. Translation: AAI05011.1.
    BC105012 mRNA. Translation: AAI05013.1.
    CCDSiCCDS3129.1. [Q9Y4C5-1]
    RefSeqiNP_004258.2. NM_004267.4. [Q9Y4C5-1]
    UniGeneiHs.529249.
    Hs.8786.

    Genome annotation databases

    EnsembliENST00000309575; ENSP00000307911; ENSG00000175040. [Q9Y4C5-1]
    GeneIDi9435.
    KEGGihsa:9435.
    UCSCiuc003evm.3. human. [Q9Y4C5-1]

    Polymorphism databases

    DMDMi61212252.

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB014679 mRNA. Translation: BAA34265.2 . Different initiation.
    AB014680 mRNA. Translation: BAA34266.2 .
    AF083066 mRNA. Translation: AAD20981.1 .
    AB021124 mRNA. Translation: BAB16886.1 . Different initiation.
    AB021125 Genomic DNA. Translation: BAB16887.1 . Different initiation.
    CH471052 Genomic DNA. Translation: EAW78952.1 .
    CH471052 Genomic DNA. Translation: EAW78953.1 .
    BC105010 mRNA. Translation: AAI05011.1 .
    BC105012 mRNA. Translation: AAI05013.1 .
    CCDSi CCDS3129.1. [Q9Y4C5-1 ]
    RefSeqi NP_004258.2. NM_004267.4. [Q9Y4C5-1 ]
    UniGenei Hs.529249.
    Hs.8786.

    3D structure databases

    ProteinModelPortali Q9Y4C5.
    SMRi Q9Y4C5. Positions 417-501.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000307911.

    PTM databases

    PhosphoSitei Q9Y4C5.

    Polymorphism databases

    DMDMi 61212252.

    Proteomic databases

    PaxDbi Q9Y4C5.
    PRIDEi Q9Y4C5.

    Protocols and materials databases

    DNASUi 9435.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000309575 ; ENSP00000307911 ; ENSG00000175040 . [Q9Y4C5-1 ]
    GeneIDi 9435.
    KEGGi hsa:9435.
    UCSCi uc003evm.3. human. [Q9Y4C5-1 ]

    Organism-specific databases

    CTDi 9435.
    GeneCardsi GC03P142838.
    HGNCi HGNC:1970. CHST2.
    HPAi HPA013313.
    MIMi 603798. gene.
    neXtProti NX_Q9Y4C5.
    PharmGKBi PA26502.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG67451.
    HOGENOMi HOG000261614.
    HOVERGENi HBG050949.
    InParanoidi Q9Y4C5.
    KOi K04745.
    OMAi MGGPADY.
    OrthoDBi EOG7RZ5S0.
    PhylomeDBi Q9Y4C5.
    TreeFami TF342871.

    Enzyme and pathway databases

    Reactomei REACT_121120. Keratan sulfate biosynthesis.
    SABIO-RK Q9Y4C5.

    Miscellaneous databases

    ChiTaRSi CHST2. human.
    GeneWikii CHST2.
    GenomeRNAii 9435.
    NextBioi 35332.
    PROi Q9Y4C5.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9Y4C5.
    CleanExi HS_CHST2.
    Genevestigatori Q9Y4C5.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR016469. Carbohydrate_sulfotransferase.
    IPR027417. P-loop_NTPase.
    IPR000863. Sulfotransferase_dom.
    [Graphical view ]
    Pfami PF00685. Sulfotransfer_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005883. Carbohydrate_sulfotransferase. 1 hit.
    SUPFAMi SSF52540. SSF52540. 3 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Human N-acetylglucosamine-6-O-sulfotransferase involved in the biosynthesis of 6-sulfo sialyl Lewis X: molecular cloning, chromosomal mapping, and expression in various organs and tumor cells."
      Uchimura K., Muramatsu H., Kaname T., Ogawa H., Yamakawa T., Fan Q.-W., Mitsuoka C., Kannagi R., Habuchi O., Yokoyama I., Yamamura K., Ozaki T., Nakagawara A., Kadomatsu K., Muramatsu T.
      J. Biochem. 124:670-678(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, ALTERNATIVE INITIATION, TISSUE SPECIFICITY.
      Tissue: Brain.
    2. Uchimura K., Muramatsu H., Muramatsu T.
      Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "CHST1 and CHST2 sulfotransferases expressed by human vascular endothelial cells: cDNA cloning, expression, and chromosomal localization."
      Li X., Tedder T.F.
      Genomics 55:345-347(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Tissue: Umbilical vein endothelial cell.
    4. "Functional expression and genomic structure of human N-acetylglucosamine-6-O-sulfotransferase that transfers sulfate to b-N-acetylglucosamine at the nonreducing end of an N-acetyllactosamine sequence."
      Sakaguchi H., Kitagawa H., Sugahara K.
      Biochim. Biophys. Acta 1523:269-276(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION.
      Tissue: Placenta.
    5. 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].
      Tissue: Brain.
    7. "CHST1 and CHST2 sulfotransferase expression by vascular endothelial cells regulates shear-resistant leukocyte rolling via L-selectin."
      Li X., Tu L., Murphy P.G., Kadono T., Steeber D.A., Tedder T.F.
      J. Leukoc. Biol. 69:565-574(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INDUCTION.
    8. "Characterization and mutagenesis of Gal/GlcNAc-6-O-sulfotransferases."
      Grunwell J.R., Rath V.L., Rasmussen J., Cabrilo Z., Bertozzi C.R.
      Biochemistry 41:15590-15600(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-174; ARG-296; LYS-304; ARG-332 AND ARG-341.
    9. "Specificities of N-acetylglucosamine-6-O-sulfotransferases in relation to L-selectin ligand synthesis and tumor-associated enzyme expression."
      Uchimura K., El-Fasakhany F.M., Hori M., Hemmerich S., Blink S.E., Kansas G.S., Kanamori A., Kumamoto K., Kannagi R., Muramatsu T.
      J. Biol. Chem. 277:3979-3984(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBSTRATE SPECIFICITY.
    10. "Golgi localization of carbohydrate sulfotransferases is a determinant of L-selectin ligand biosynthesis."
      de Graffenried C.L., Bertozzi C.R.
      J. Biol. Chem. 278:40282-40295(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    11. "Role of the carboxyl-terminal region in the activity of N-acetylglucosamine 6-o-sulfotransferase-1."
      Chen L., Ichihara-Tanaka K., Muramatsu T.
      J. Biochem. 136:659-664(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LYS-518; ASP-519; LEU-520; SER-521; LYS-522; THR-523; LEU-524; LEU-525; ARG-526; LYS-527; PRO-528; ARG-529 AND LEU-530.
    12. "The stem region of the sulfotransferase GlcNAc6ST-1 is a determinant of substrate specificity."
      de Graffenried C.L., Bertozzi C.R.
      J. Biol. Chem. 279:40035-40043(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, MUTAGENESIS OF CYS-59 AND CYS-86.
    13. "Effects of N-glycosylation on the activity and localization of GlcNAc-6-sulfotransferase 1."
      Desko M.M., Gross D.A., Kohler J.J.
      Glycobiology 19:1068-1077(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-243; ASN-457 AND ASN-475, ABSENCE OF GLYCOSYLATION AT ASN-152, MUTAGENESIS OF ASN-457 AND ASN-475.
    14. "Expression of long-form N-acetylglucosamine-6-O-sulfotransferase 1 in human high endothelial venules."
      Fujiwara M., Kobayashi M., Hoshino H., Uchimura K., Nakada T., Masumoto J., Sakai Y., Fukuda M., Nakayama J.
      J. Histochem. Cytochem. 60:397-407(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, SUBUNIT, ALTERNATIVE INITIATION.

    Entry informationi

    Entry nameiCHST2_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y4C5
    Secondary accession number(s): D3DNG5
    , Q2M370, Q9GZN5, Q9UED5, Q9Y6F2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 108 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, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3