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)

O00587

- MFNG_HUMAN

UniProt

O00587 - MFNG_HUMAN

Protein

Beta-1,3-N-acetylglucosaminyltransferase manic fringe

Gene

MFNG

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 117 (01 Oct 2014)
      Sequence version 2 (27 Mar 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Glycosyltransferase involved in the elongation of O-linked ligands to activate Notch signaling. Possesses fucose-specific beta-1,3-N-acetylglucosaminyltransferase activity.1 Publication

    Catalytic activityi

    Transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor.1 Publication

    Cofactori

    Manganese.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei70 – 701SubstrateBy similarity
    Binding sitei143 – 1431SubstrateBy similarity
    Metal bindingi144 – 1441ManganeseBy similarity
    Active sitei232 – 2321By similarity
    Metal bindingi256 – 2561ManganeseBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. pattern specification process Source: ProtInc
    2. positive regulation of Notch signaling pathway Source: Ensembl
    3. positive regulation of protein binding Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein, Glycosyltransferase, Transferase

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_118798. Pre-NOTCH Processing in Golgi.
    SignaLinkiO00587.

    Protein family/group databases

    CAZyiGT31. Glycosyltransferase Family 31.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-1,3-N-acetylglucosaminyltransferase manic fringe (EC:2.4.1.222)
    Alternative name(s):
    O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase
    Gene namesi
    Name:MFNG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:7038. MFNG.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: ProtInc
    2. integral component of Golgi membrane Source: InterPro

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30775.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 321321Beta-1,3-N-acetylglucosaminyltransferase manic fringePRO_0000219182Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi109 – 1091N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi110 ↔ 121By similarity
    Disulfide bondi139 ↔ 202By similarity
    Glycosylationi185 – 1851N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi306 ↔ 315By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiO00587.
    PRIDEiO00587.

    Expressioni

    Gene expression databases

    ArrayExpressiO00587.
    BgeeiO00587.
    CleanExiHS_MFNG.
    GenevestigatoriO00587.

    Organism-specific databases

    HPAiHPA048936.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000349490.

    Structurei

    3D structure databases

    ProteinModelPortaliO00587.
    SMRiO00587. Positions 50-318.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 77CytoplasmicSequence Analysis
    Topological domaini28 – 321294LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei8 – 2720Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyltransferase 31 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG70217.
    HOGENOMiHOG000046678.
    HOVERGENiHBG007986.
    InParanoidiO00587.
    KOiK05948.
    OMAiLRWFCHV.
    OrthoDBiEOG7ZSHTD.
    PhylomeDBiO00587.
    TreeFamiTF324207.

    Family and domain databases

    InterProiIPR017374. Fringe.
    IPR003378. Fringe-like.
    [Graphical view]
    PfamiPF02434. Fringe. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038073. B-acetylgalactosaminyltfrase. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O00587-1) [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

    MQCRLPRGLA GALLTLLCMG LLCLRYHLNL SPQRVQGTPE LSQPNPGPPK    50
    LQLHDVFIAV KTTRAFHRLR LELLLDTWVS RTREQTFVFT DSPDKGLQER 100
    LGSHLVVTNC SAEHSHPALS CKMAAEFDTF LASGLRWFCH VDDDNYVNPR 150
    ALLQLLRAFP LARDVYVGRP SLNRPIHASE PQPHNRTRLV QFWFATGGAG 200
    FCINRKLALK MAPWASGSRF MDTSALIRLP DDCTMGYIIE CKLGGRLQPS 250
    PLFHSHLETL QLLRTAQLPE QVTLSYGVFE GKLNVIKLQG PFSPEEDPSR 300
    FRSLHCLLYP DTPWCPQLGA R 321
    Length:321
    Mass (Da):36,202
    Last modified:March 27, 2002 - v2
    Checksum:i7CB847E7423DD0BC
    GO
    Isoform 2 (identifier: O00587-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         86-102: TFVFTDSPDKGLQERLG → VTR

    Note: No experimental confirmation available.

    Show »
    Length:307
    Mass (Da):34,666
    Checksum:i62DAF2173EA15DB6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti85 – 851Q → L in AAC51358. (PubMed:9187150)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti302 – 3021R → C.
    Corresponds to variant rs8192548 [ dbSNP | Ensembl ].
    VAR_024467

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei86 – 10217TFVFT…QERLG → VTR in isoform 2. 1 PublicationVSP_042857Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U94352 mRNA. Translation: AAC51358.1.
    CR456518 mRNA. Translation: CAG30404.1.
    AK297149 mRNA. Translation: BAG59648.1.
    Z93096 Genomic DNA. Translation: CAB07511.1.
    BC094814 mRNA. Translation: AAH94814.1.
    CCDSiCCDS13947.1. [O00587-1]
    CCDS54525.1. [O00587-2]
    RefSeqiNP_001159815.1. NM_001166343.1. [O00587-2]
    NP_002396.2. NM_002405.3. [O00587-1]
    UniGeneiHs.517603.

    Genome annotation databases

    EnsembliENST00000356998; ENSP00000349490; ENSG00000100060. [O00587-1]
    ENST00000416983; ENSP00000413855; ENSG00000100060. [O00587-2]
    GeneIDi4242.
    KEGGihsa:4242.
    UCSCiuc003ass.2. human. [O00587-1]
    uc011anj.2. human. [O00587-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Functional Glycomics Gateway - GTase

    Beta-1,3-N-acetylglucosaminyltransferase manic fringe

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U94352 mRNA. Translation: AAC51358.1 .
    CR456518 mRNA. Translation: CAG30404.1 .
    AK297149 mRNA. Translation: BAG59648.1 .
    Z93096 Genomic DNA. Translation: CAB07511.1 .
    BC094814 mRNA. Translation: AAH94814.1 .
    CCDSi CCDS13947.1. [O00587-1 ]
    CCDS54525.1. [O00587-2 ]
    RefSeqi NP_001159815.1. NM_001166343.1. [O00587-2 ]
    NP_002396.2. NM_002405.3. [O00587-1 ]
    UniGenei Hs.517603.

    3D structure databases

    ProteinModelPortali O00587.
    SMRi O00587. Positions 50-318.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000349490.

    Protein family/group databases

    CAZyi GT31. Glycosyltransferase Family 31.

    Proteomic databases

    PaxDbi O00587.
    PRIDEi O00587.

    Protocols and materials databases

    DNASUi 4242.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356998 ; ENSP00000349490 ; ENSG00000100060 . [O00587-1 ]
    ENST00000416983 ; ENSP00000413855 ; ENSG00000100060 . [O00587-2 ]
    GeneIDi 4242.
    KEGGi hsa:4242.
    UCSCi uc003ass.2. human. [O00587-1 ]
    uc011anj.2. human. [O00587-2 ]

    Organism-specific databases

    CTDi 4242.
    GeneCardsi GC22M037865.
    H-InvDB HIX0041190.
    HGNCi HGNC:7038. MFNG.
    HPAi HPA048936.
    MIMi 602577. gene.
    neXtProti NX_O00587.
    PharmGKBi PA30775.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG70217.
    HOGENOMi HOG000046678.
    HOVERGENi HBG007986.
    InParanoidi O00587.
    KOi K05948.
    OMAi LRWFCHV.
    OrthoDBi EOG7ZSHTD.
    PhylomeDBi O00587.
    TreeFami TF324207.

    Enzyme and pathway databases

    Reactomei REACT_118798. Pre-NOTCH Processing in Golgi.
    SignaLinki O00587.

    Miscellaneous databases

    GeneWikii MFNG.
    GenomeRNAii 4242.
    NextBioi 16729.
    PROi O00587.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00587.
    Bgeei O00587.
    CleanExi HS_MFNG.
    Genevestigatori O00587.

    Family and domain databases

    InterProi IPR017374. Fringe.
    IPR003378. Fringe-like.
    [Graphical view ]
    Pfami PF02434. Fringe. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038073. B-acetylgalactosaminyltfrase. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "A family of mammalian Fringe genes implicated in boundary determination and the Notch pathway."
      Johnston S.H., Rauskolb C., Wilson R., Prabhakaran B., Irvine K.D., Vogt T.F.
      Development 124:2245-2254(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "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] (ISOFORM 2).
    4. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [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] (ISOFORM 1).
      Tissue: Lymph.
    6. Cited for: FUNCTION, CATALYTIC ACTIVITY.

    Entry informationi

    Entry nameiMFNG_HUMAN
    AccessioniPrimary (citable) accession number: O00587
    Secondary accession number(s): B4DLT6, O43730, Q504S9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 27, 2002
    Last sequence update: March 27, 2002
    Last modified: October 1, 2014
    This is version 117 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 22
      Human chromosome 22: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3