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O00587

- MFNG_HUMAN

UniProt

O00587 - MFNG_HUMAN

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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

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

Mn2+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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 77CytoplasmicSequence Analysis
Transmembranei8 – 2720Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini28 – 321294LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

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

BgeeiO00587.
CleanExiHS_MFNG.
ExpressionAtlasiO00587. baseline and differential.
GenevestigatoriO00587.

Organism-specific databases

HPAiHPA048936.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000349490.

Structurei

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 31 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG70217.
GeneTreeiENSGT00390000009913.
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

        10         20         30         40         50
MQCRLPRGLA GALLTLLCMG LLCLRYHLNL SPQRVQGTPE LSQPNPGPPK
60 70 80 90 100
LQLHDVFIAV KTTRAFHRLR LELLLDTWVS RTREQTFVFT DSPDKGLQER
110 120 130 140 150
LGSHLVVTNC SAEHSHPALS CKMAAEFDTF LASGLRWFCH VDDDNYVNPR
160 170 180 190 200
ALLQLLRAFP LARDVYVGRP SLNRPIHASE PQPHNRTRLV QFWFATGGAG
210 220 230 240 250
FCINRKLALK MAPWASGSRF MDTSALIRLP DDCTMGYIIE CKLGGRLQPS
260 270 280 290 300
PLFHSHLETL QLLRTAQLPE QVTLSYGVFE GKLNVIKLQG PFSPEEDPSR
310 320
FRSLHCLLYP DTPWCPQLGA R
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
GeneTreei ENSGT00390000009913.
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

Bgeei O00587.
CleanExi HS_MFNG.
ExpressionAtlasi O00587. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 119 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