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Q8N3T1

- GLT15_HUMAN

UniProt

Q8N3T1 - GLT15_HUMAN

Protein

Polypeptide N-acetylgalactosaminyltransferase 15

Gene

GALNT15

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 2 (16 Aug 2004)
      Previous versions | rss
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    Functioni

    Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Although it displays a much weaker activity toward all substrates tested compared to GALNT2, it is able to transfer up to seven GalNAc residues to the Muc5AC peptide, suggesting that it can fill vicinal Thr/Ser residues in cooperation with other GALNT proteins. Prefers Muc1a as substrate.

    Catalytic activityi

    UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.1 Publication

    Cofactori

    Manganese.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei231 – 2311SubstrateBy similarity
    Binding sitei260 – 2601SubstrateBy similarity
    Metal bindingi283 – 2831ManganeseBy similarity
    Metal bindingi285 – 2851ManganeseBy similarity
    Metal bindingi417 – 4171ManganeseBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. polypeptide N-acetylgalactosaminyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. O-glycan processing Source: Reactome
    3. post-translational protein modification Source: Reactome

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Ligandi

    Lectin, Manganese, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_115606. O-linked glycosylation of mucins.
    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiCBM13. Carbohydrate-Binding Module Family 13.
    GT27. Glycosyltransferase Family 27.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polypeptide N-acetylgalactosaminyltransferase 15 (EC:2.4.1.41)
    Alternative name(s):
    Polypeptide GalNAc transferase-like protein 2
    Short name:
    GalNAc-T-like protein 2
    Short name:
    pp-GaNTase-like protein 2
    Polypeptide N-acetylgalactosaminyltransferase-like protein 2
    Protein-UDP acetylgalactosaminyltransferase-like protein 2
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 2
    Gene namesi
    Name:GALNT15
    Synonyms:GALNTL2
    ORF Names:UNQ770/PRO1564
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:21531. GALNT15.

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi membrane Source: Reactome
    2. integral component of membrane Source: UniProtKB-KW
    3. transport vesicle Source: LIFEdb

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134936170.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 639639Polypeptide N-acetylgalactosaminyltransferase 15PRO_0000059137Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi107 – 1071N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi181 ↔ 412PROSITE-ProRule annotation
    Disulfide bondi403 ↔ 482PROSITE-ProRule annotation
    Disulfide bondi517 ↔ 536PROSITE-ProRule annotation
    Disulfide bondi562 ↔ 575PROSITE-ProRule annotation
    Glycosylationi574 – 5741N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi603 ↔ 620PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ8N3T1.
    PRIDEiQ8N3T1.

    PTM databases

    PhosphoSiteiQ8N3T1.

    Expressioni

    Tissue specificityi

    Widely expressed. Highly expressed in small intestine, placenta, spleen, cerebral cortex and ovary. Expressed at intermediate level in uterus, mammary gland, stomach, cerebellum and whole brain. Weakly expressed in fetal brain, bone marrow, thyroid gland, thymus, heart, skeletal muscle, lung, liver, colon, pancreas, kidney and testis. Not expressed in leukocyte. Expressed in both normal and osteoarthritic cartilage. Expressed at low level in chondrocytes in all zones of both normal and osteoarthritic cartilage.2 Publications

    Gene expression databases

    ArrayExpressiQ8N3T1.
    BgeeiQ8N3T1.
    CleanExiHS_GALNTL2.
    GenevestigatoriQ8N3T1.

    Organism-specific databases

    HPAiHPA017076.

    Interactioni

    Protein-protein interaction databases

    BioGridi125583. 1 interaction.
    IntActiQ8N3T1. 1 interaction.
    MINTiMINT-4724072.
    STRINGi9606.ENSP00000344260.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8N3T1.
    SMRiQ8N3T1. Positions 595-631.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1111CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini35 – 639605LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei12 – 3423Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini504 – 631128Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni190 – 299110Catalytic subdomain AAdd
    BLAST
    Regioni358 – 42063Catalytic subdomain BAdd
    BLAST

    Domaini

    There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.By similarity
    The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.By similarity

    Sequence similaritiesi

    Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG282033.
    HOGENOMiHOG000038227.
    HOVERGENiHBG051699.
    InParanoidiQ8N3T1.
    KOiK00710.
    OMAiETWLGSF.
    PhylomeDBiQ8N3T1.
    TreeFamiTF313267.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    InterProiIPR001173. Glyco_trans_2-like.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR000772. Ricin_B_lectin.
    [Graphical view]
    PfamiPF00535. Glycos_transf_2. 1 hit.
    PF00652. Ricin_B_lectin. 1 hit.
    [Graphical view]
    SMARTiSM00458. RICIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF50370. SSF50370. 1 hit.
    SSF53448. SSF53448. 1 hit.
    PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8N3T1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLLRKRYRHR PCRLQFLLLL LMLGCVLMMV AMLHPPHHTL HQTVTAQASK    50
    HSPEARYRLD FGESQDWVLE AEDEGEEYSP LEGLPPFISL REDQLLVAVA 100
    LPQARRNQSQ GRRGGSYRLI KQPRRQDKEA PKRDWGADED GEVSEEEELT 150
    PFSLDPRGLQ EALSARIPLQ RALPEVRHPL CLQQHPQDSL PTASVILCFH 200
    DEAWSTLLRT VHSILDTVPR AFLKEIILVD DLSQQGQLKS ALSEYVARLE 250
    GVKLLRSNKR LGAIRARMLG ATRATGDVLV FMDAHCECHP GWLEPLLSRI 300
    AGDRSRVVSP VIDVIDWKTF QYYPSKDLQR GVLDWKLDFH WEPLPEHVRK 350
    ALQSPISPIR SPVVPGEVVA MDRHYFQNTG AYDSLMSLRG GENLELSFKA 400
    WLCGGSVEIL PCSRVGHIYQ NQDSHSPLDQ EATLRNRVRI AETWLGSFKE 450
    TFYKHSPEAF SLSKAEKPDC MERLQLQRRL GCRTFHWFLA NVYPELYPSE 500
    PRPSFSGKLH NTGLGLCADC QAEGDILGCP MVLAPCSDSR QQQYLQHTSR 550
    KEIHFGSPQH LCFAVRQEQV ILQNCTEEGL AIHQQHWDFQ ENGMIVHILS 600
    GKCMEAVVQE NNKDLYLRPC DGKARQQWRF DQINAVDER 639
    Length:639
    Mass (Da):73,063
    Last modified:August 16, 2004 - v2
    Checksum:iF5DCA523AF4965DA
    GO

    Sequence cautioni

    The sequence CAD89983.1 differs from that shown. Reason: Frameshift at positions 169, 192, 206, 222 and 270.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti44 – 441V → D in CAD38585. (PubMed:17974005)Curated
    Sequence conflicti326 – 3261K → R in CAD89983. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti68 – 681V → G.
    Corresponds to variant rs36026882 [ dbSNP | Ensembl ].
    VAR_049243
    Natural varianti151 – 1511P → L.
    Corresponds to variant rs11715981 [ dbSNP | Ensembl ].
    VAR_049244
    Natural varianti324 – 3241P → A.
    Corresponds to variant rs12634179 [ dbSNP | Ensembl ].
    VAR_049245
    Natural varianti432 – 4321A → T.2 Publications
    Corresponds to variant rs17851238 [ dbSNP | Ensembl ].
    VAR_049246
    Natural varianti510 – 5101H → Y.
    Corresponds to variant rs2271077 [ dbSNP | Ensembl ].
    VAR_019593

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB078149 mRNA. Translation: BAD29961.1.
    AY035399 mRNA. Translation: AAK63127.1.
    AY358443 mRNA. Translation: AAQ88808.1.
    AK312425 mRNA. Translation: BAG35335.1.
    AL831925 mRNA. Translation: CAD38585.1.
    AL832575 mRNA. Translation: CAD89983.1. Frameshift.
    AC087858 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW64266.1.
    BC014789 mRNA. Translation: AAH14789.1.
    CCDSiCCDS33711.1.
    RefSeqiNP_473451.3. NM_054110.4.
    UniGeneiHs.411308.

    Genome annotation databases

    EnsembliENST00000339732; ENSP00000344260; ENSG00000131386.
    GeneIDi117248.
    KEGGihsa:117248.
    UCSCiuc003caq.4. human.

    Polymorphism databases

    DMDMi51316023.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Functional Glycomics Gateway - GTase

    Polypeptide N-acetylgalactosaminyltransferase-like protein 2

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB078149 mRNA. Translation: BAD29961.1 .
    AY035399 mRNA. Translation: AAK63127.1 .
    AY358443 mRNA. Translation: AAQ88808.1 .
    AK312425 mRNA. Translation: BAG35335.1 .
    AL831925 mRNA. Translation: CAD38585.1 .
    AL832575 mRNA. Translation: CAD89983.1 . Frameshift.
    AC087858 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW64266.1 .
    BC014789 mRNA. Translation: AAH14789.1 .
    CCDSi CCDS33711.1.
    RefSeqi NP_473451.3. NM_054110.4.
    UniGenei Hs.411308.

    3D structure databases

    ProteinModelPortali Q8N3T1.
    SMRi Q8N3T1. Positions 595-631.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125583. 1 interaction.
    IntActi Q8N3T1. 1 interaction.
    MINTi MINT-4724072.
    STRINGi 9606.ENSP00000344260.

    Protein family/group databases

    CAZyi CBM13. Carbohydrate-Binding Module Family 13.
    GT27. Glycosyltransferase Family 27.

    PTM databases

    PhosphoSitei Q8N3T1.

    Polymorphism databases

    DMDMi 51316023.

    Proteomic databases

    PaxDbi Q8N3T1.
    PRIDEi Q8N3T1.

    Protocols and materials databases

    DNASUi 117248.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000339732 ; ENSP00000344260 ; ENSG00000131386 .
    GeneIDi 117248.
    KEGGi hsa:117248.
    UCSCi uc003caq.4. human.

    Organism-specific databases

    CTDi 117248.
    GeneCardsi GC03P016216.
    HGNCi HGNC:21531. GALNT15.
    HPAi HPA017076.
    neXtProti NX_Q8N3T1.
    PharmGKBi PA134936170.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG282033.
    HOGENOMi HOG000038227.
    HOVERGENi HBG051699.
    InParanoidi Q8N3T1.
    KOi K00710.
    OMAi ETWLGSF.
    PhylomeDBi Q8N3T1.
    TreeFami TF313267.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    Reactomei REACT_115606. O-linked glycosylation of mucins.

    Miscellaneous databases

    GeneWikii GALNTL2.
    GenomeRNAii 117248.
    NextBioi 80182.
    PROi Q8N3T1.

    Gene expression databases

    ArrayExpressi Q8N3T1.
    Bgeei Q8N3T1.
    CleanExi HS_GALNTL2.
    Genevestigatori Q8N3T1.

    Family and domain databases

    Gene3Di 3.90.550.10. 1 hit.
    InterProi IPR001173. Glyco_trans_2-like.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR000772. Ricin_B_lectin.
    [Graphical view ]
    Pfami PF00535. Glycos_transf_2. 1 hit.
    PF00652. Ricin_B_lectin. 1 hit.
    [Graphical view ]
    SMARTi SM00458. RICIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50370. SSF50370. 1 hit.
    SSF53448. SSF53448. 1 hit.
    PROSITEi PS50231. RICIN_B_LECTIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY.
    2. "Identification and initial characterization of 5000 expressed sequenced tags (ESTs) each from adult human normal and osteoarthritic cartilage cDNA libraries."
      Kumar S., Connor J.R., Dodds R.A., Halsey W., Van Horn M., Mao J., Sathe G.M., Mui P., Agarwal P., Badger A.M., Lee J.C., Gowen M., Lark M.W.
      Osteoarthritis Cartilage 9:641-653(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], TISSUE SPECIFICITY.
      Tissue: Osteoarthritic cartilage.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-432.
      Tissue: Adipose tissue and Spinal cord.
    6. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT THR-432.
    8. "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.

    Entry informationi

    Entry nameiGLT15_HUMAN
    AccessioniPrimary (citable) accession number: Q8N3T1
    Secondary accession number(s): A6NMN1
    , B2R638, F1LIP6, Q86T60, Q96C46, Q96DJ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: August 16, 2004
    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

    Caution

    Was originally termed Galnt15/pp-GaNTase 15.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3