Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q3V5L5

- MGT5B_HUMAN

UniProt

Q3V5L5 - MGT5B_HUMAN

Protein

Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase B

Gene

MGAT5B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 2 (29 May 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Glycosyltransferase that acts on alpha-linked mannose of N-glycans and O-mannosyl glycans. Catalyzes the transfer of N-acetylglucosamine (GlcNAc) to the beta 1-6 linkage of the mannose residue of GlcNAcbeta1,2-Manalpha on both the alpha1,3- and alpha1,6-linked mannose arms in the core structure of N-glycan. Also acts on the GlcNAcbeta1,2-Manalpha1-Ser/Thr moiety, forming a 2,6-branched structure in brain O-mannosyl glycan. Plays an active role in modulating integrin and laminin-dependent adhesion and migration of neuronal cells via its activity in the O-mannosyl glycan pathway.5 Publications

    Catalytic activityi

    UDP-N-acetyl-D-glucosamine + 6-(2-(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl)-beta-D-mannosyl-R = UDP + 6-(2,6-bis(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl)-beta-D-mannosyl-R.2 Publications

    Pathwayi

    GO - Molecular functioni

    1. alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: IntAct

    GO - Biological processi

    1. protein N-linked glycosylation Source: InterPro

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Ligandi

    Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS15606-MONOMER.
    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGT18. Glycosyltransferase Family 18.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase B (EC:2.4.1.-, EC:2.4.1.155)
    Alternative name(s):
    Alpha-mannoside beta-1,6-N-acetylglucosaminyltransferase B
    GlcNAc-T Vb
    Short name:
    GNT-Vb
    Short name:
    hGnTVb
    Mannoside acetylglucosaminyltransferase 5B
    N-acetylglucosaminyl-transferase Vb
    N-acetylglucosaminyltransferase IX
    Short name:
    GNT-IX
    Gene namesi
    Name:MGAT5B
    Synonyms:KIAA2008
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:24140. MGAT5B.

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134987427.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 792792Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase BPRO_0000288611Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi127 – 1271N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ3V5L5.
    PaxDbiQ3V5L5.
    PRIDEiQ3V5L5.

    Expressioni

    Tissue specificityi

    Predominantly expressed in brain. Expressed in all area of the adult and fetal brain Also expressed at much lower level in testis, spleen and thymus.2 Publications

    Gene expression databases

    ArrayExpressiQ3V5L5.
    BgeeiQ3V5L5.
    CleanExiHS_MGAT5B.
    GenevestigatoriQ3V5L5.

    Organism-specific databases

    HPAiHPA017424.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Hoxa1P090223EBI-3957727,EBI-3957603From a different organism.

    Protein-protein interaction databases

    BioGridi127000. 2 interactions.
    IntActiQ3V5L5. 2 interactions.
    STRINGi9606.ENSP00000391227.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3V5L5.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2424CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini46 – 792747LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei25 – 4521Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyltransferase 18 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG270839.
    HOGENOMiHOG000006557.
    HOVERGENiHBG052469.
    InParanoidiQ3V5L5.
    KOiK09661.
    OMAiNHLYPAF.
    OrthoDBiEOG71K629.
    PhylomeDBiQ3V5L5.
    TreeFamiTF313714.

    Family and domain databases

    InterProiIPR026116. GlyclTrfase_18.
    [Graphical view]
    PANTHERiPTHR15075. PTHR15075. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q3V5L5-1) [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

    MITVNPDGKI MVRRCLVTLR PFRLFVLGIG FFTLCFLMTS LGGQFSARRL    50
    GDSPFTIRTE VMGGPESRGV LRKMSDLLEL MVKRMDALAR LENSSELHRA 100
    GGDLHFPADR MPPGAGLMER IQAIAQNVSD IAVKVDQILR HSLLLHSKVS 150
    EGRRDQCEAP SDPKFPDCSG KVEWMRARWT SDPCYAFFGV DGTECSFLIY 200
    LSEVEWFCPP LPWRNQTAAQ RAPKPLPKVQ AVFRSNLSHL LDLMGSGKES 250
    LIFMKKRTKR LTAQWALAAQ RLAQKLGATQ RDQKQILVHI GFLTEESGDV 300
    FSPRVLKGGP LGEMVQWADI LTALYVLGHG LRVTVSLKEL QSNLGVPPGR 350
    GSCPLTMPLP FDLIYTDYHG LQQMKRHMGL SFKKYRCRIR VIDTFGTEPA 400
    YNHEEYATLH GYRTNWGYWN LNPKQFMTMF PHTPDNSFMG FVSEELNETE 450
    KRLIKGGKAS NMAVVYGKEA SIWKLQGKEK FLGILNKYME IHGTVYYESQ 500
    RPPEVPAFVK NHGLLPQPEF QQLLRKAKLF IGFGFPYEGP APLEAIANGC 550
    IFLQSRFSPP HSSLNHEFFR GKPTSREVFS QHPYAENFIG KPHVWTVDYN 600
    NSEEFEAAIK AIMRTQVDPY LPYEYTCEGM LERIHAYIQH QDFCRAPDPA 650
    LPEAHAPQSP FVLAPNATHL EWARNTSLAP GAWPPAHALR AWLAVPGRAC 700
    TDTCLDHGLI CEPSFFPFLN SQDAFLKLQV PCDSTESEMN HLYPAFAQPG 750
    QECYLQKEPL LFSCAGSNTK YRRLCPCRDF RKGQVALCQG CL 792
    Length:792
    Mass (Da):89,535
    Last modified:May 29, 2007 - v2
    Checksum:iC2EB9445FDBE9429
    GO
    Isoform 2 (identifier: Q3V5L5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-22: MITVNPDGKIMVRRCLVTLRPF → MHSFVKHLCSRYVVERQGTMALPALLTRLLPLR
         475-476: Missing.

    Show »
    Length:801
    Mass (Da):90,571
    Checksum:iB5EC03A96DBFB38B
    GO
    Isoform 3 (identifier: Q3V5L5-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         475-476: Missing.

    Show »
    Length:790
    Mass (Da):89,294
    Checksum:i22193B688EFFACFF
    GO

    Sequence cautioni

    The sequence AAH62354.1 differs from that shown. Reason: Probable cloning artifact.
    The sequence AAH63862.1 differs from that shown. Reason: Probable cloning artifact.
    The sequence BAB71598.1 differs from that shown. Reason: Chimeric sequence.
    The sequence BAD02406.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAE44474.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti70 – 701V → I.
    Corresponds to variant rs571264 [ dbSNP | Ensembl ].
    VAR_032452

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2222MITVN…TLRPF → MHSFVKHLCSRYVVERQGTM ALPALLTRLLPLR in isoform 2. 1 PublicationVSP_025731Add
    BLAST
    Alternative sequencei475 – 4762Missing in isoform 2 and isoform 3. 1 PublicationVSP_025734

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB114297 mRNA. Translation: BAD02406.1. Different initiation.
    AB109185 mRNA. Translation: BAC84969.1.
    AB235153 mRNA. Translation: BAE44474.1. Different initiation.
    AC016168 Genomic DNA. No translation available.
    BC062354 mRNA. Translation: AAH62354.1. Sequence problems.
    BC063862 mRNA. Translation: AAH63862.1. Sequence problems.
    AK057861 mRNA. Translation: BAB71598.1. Sequence problems.
    CCDSiCCDS11751.1. [Q3V5L5-5]
    CCDS45788.1. [Q3V5L5-2]
    CCDS59299.1. [Q3V5L5-1]
    RefSeqiNP_001186101.1. NM_001199172.1. [Q3V5L5-1]
    NP_653278.2. NM_144677.2. [Q3V5L5-5]
    NP_945193.1. NM_198955.1. [Q3V5L5-2]
    UniGeneiHs.144531.

    Genome annotation databases

    EnsembliENST00000301618; ENSP00000301618; ENSG00000167889. [Q3V5L5-5]
    ENST00000428789; ENSP00000391227; ENSG00000167889. [Q3V5L5-2]
    ENST00000569840; ENSP00000456037; ENSG00000167889. [Q3V5L5-1]
    GeneIDi146664.
    KEGGihsa:146664.
    UCSCiuc002jth.3. human. [Q3V5L5-5]
    uc002jti.3. human. [Q3V5L5-2]
    uc031rem.1. human. [Q3V5L5-1]

    Polymorphism databases

    DMDMi152040009.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB114297 mRNA. Translation: BAD02406.1 . Different initiation.
    AB109185 mRNA. Translation: BAC84969.1 .
    AB235153 mRNA. Translation: BAE44474.1 . Different initiation.
    AC016168 Genomic DNA. No translation available.
    BC062354 mRNA. Translation: AAH62354.1 . Sequence problems.
    BC063862 mRNA. Translation: AAH63862.1 . Sequence problems.
    AK057861 mRNA. Translation: BAB71598.1 . Sequence problems.
    CCDSi CCDS11751.1. [Q3V5L5-5 ]
    CCDS45788.1. [Q3V5L5-2 ]
    CCDS59299.1. [Q3V5L5-1 ]
    RefSeqi NP_001186101.1. NM_001199172.1. [Q3V5L5-1 ]
    NP_653278.2. NM_144677.2. [Q3V5L5-5 ]
    NP_945193.1. NM_198955.1. [Q3V5L5-2 ]
    UniGenei Hs.144531.

    3D structure databases

    ProteinModelPortali Q3V5L5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 127000. 2 interactions.
    IntActi Q3V5L5. 2 interactions.
    STRINGi 9606.ENSP00000391227.

    Protein family/group databases

    CAZyi GT18. Glycosyltransferase Family 18.

    Polymorphism databases

    DMDMi 152040009.

    Proteomic databases

    MaxQBi Q3V5L5.
    PaxDbi Q3V5L5.
    PRIDEi Q3V5L5.

    Protocols and materials databases

    DNASUi 146664.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000301618 ; ENSP00000301618 ; ENSG00000167889 . [Q3V5L5-5 ]
    ENST00000428789 ; ENSP00000391227 ; ENSG00000167889 . [Q3V5L5-2 ]
    ENST00000569840 ; ENSP00000456037 ; ENSG00000167889 . [Q3V5L5-1 ]
    GeneIDi 146664.
    KEGGi hsa:146664.
    UCSCi uc002jth.3. human. [Q3V5L5-5 ]
    uc002jti.3. human. [Q3V5L5-2 ]
    uc031rem.1. human. [Q3V5L5-1 ]

    Organism-specific databases

    CTDi 146664.
    GeneCardsi GC17P074864.
    HGNCi HGNC:24140. MGAT5B.
    HPAi HPA017424.
    MIMi 612441. gene.
    neXtProti NX_Q3V5L5.
    PharmGKBi PA134987427.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG270839.
    HOGENOMi HOG000006557.
    HOVERGENi HBG052469.
    InParanoidi Q3V5L5.
    KOi K09661.
    OMAi NHLYPAF.
    OrthoDBi EOG71K629.
    PhylomeDBi Q3V5L5.
    TreeFami TF313714.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    BioCyci MetaCyc:HS15606-MONOMER.

    Miscellaneous databases

    ChiTaRSi MGAT5B. human.
    GeneWikii MGAT5B.
    GenomeRNAii 146664.
    NextBioi 85408.
    PROi Q3V5L5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q3V5L5.
    Bgeei Q3V5L5.
    CleanExi HS_MGAT5B.
    Genevestigatori Q3V5L5.

    Family and domain databases

    InterProi IPR026116. GlyclTrfase_18.
    [Graphical view ]
    PANTHERi PTHR15075. PTHR15075. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ENZYME ACTIVITY, FUNCTION, TISSUE SPECIFICITY.
    2. "Molecular cloning and characterization of human GnT-IX, a novel beta1,6-N-acetylglucosaminyltransferase that is specifically expressed in the brain."
      Inamori K., Endo T., Ide Y., Fujii S., Gu J., Honke K., Taniguchi N.
      J. Biol. Chem. 278:43102-43109(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, FUNCTION, TISSUE SPECIFICITY.
      Tissue: Brain.
    3. "The nucleotide sequence of a long cDNA clone isolated from human."
      Nagase T., Kikuno R., Ohara O.
      Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    4. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] OF 1-341 (ISOFORMS 1/3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 616-792.
      Tissue: PNS and Skin.
    6. "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] OF 100-306.
      Tissue: Brain.
    7. "N-Acetylglucosaminyltransferase IX acts on the GlcNAc beta 1,2-Man alpha 1-Ser/Thr moiety, forming a 2,6-branched structure in brain O-mannosyl glycan."
      Inamori K., Endo T., Gu J., Matsuo I., Ito Y., Fujii S., Iwasaki H., Narimatsu H., Miyoshi E., Honke K., Taniguchi N.
      J. Biol. Chem. 279:2337-2340(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Integrin-dependent neuroblastoma cell adhesion and migration on laminin is regulated by expression levels of two enzymes in the O-mannosyl-linked glycosylation pathway, PomGnT1 and GnT-Vb."
      Abbott K.L., Troupe K., Lee I., Pierce M.
      Exp. Cell Res. 312:2837-2850(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "N-acetylglucosaminyltransferase VB expression enhances beta1 integrin-dependent PC12 neurite outgrowth on laminin and collagen."
      Lee I., Guo H.-B., Kamar M., Abbott K., Troupe K., Lee J.-K., Alvarez-Manilla G., Pierce M.
      J. Neurochem. 97:947-956(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiMGT5B_HUMAN
    AccessioniPrimary (citable) accession number: Q3V5L5
    Secondary accession number(s): Q6P3S8
    , Q6P6B3, Q766X5, Q76D04, Q96LS2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 29, 2007
    Last sequence update: May 29, 2007
    Last modified: October 1, 2014
    This is version 86 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 17
      Human chromosome 17: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3