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O00587 (MFNG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-1,3-N-acetylglucosaminyltransferase manic fringe

EC=2.4.1.222
Alternative name(s):
O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase
Gene names
Name:MFNG
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length321 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Glycosyltransferase involved in the elongation of O-linked ligands to activate Notch signaling. Possesses fucose-specific beta-1,3-N-acetylglucosaminyltransferase activity. Ref.6

Catalytic activity

Transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor. Ref.6

Cofactor

Manganese By similarity.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein By similarity.

Sequence similarities

Belongs to the glycosyltransferase 31 family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O00587-1)

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.
Isoform 2 (identifier: O00587-2)

The sequence of this isoform differs from the canonical sequence as follows:
     86-102: TFVFTDSPDKGLQERLG → VTR
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 321321Beta-1,3-N-acetylglucosaminyltransferase manic fringe
PRO_0000219182

Regions

Topological domain1 – 77Cytoplasmic Potential
Transmembrane8 – 2720Helical; Signal-anchor for type II membrane protein; Potential
Topological domain28 – 321294Lumenal Potential

Sites

Active site2321 By similarity
Metal binding1441Manganese By similarity
Metal binding2561Manganese By similarity
Binding site701Substrate By similarity
Binding site1431Substrate By similarity

Amino acid modifications

Glycosylation1091N-linked (GlcNAc...) Potential
Glycosylation1851N-linked (GlcNAc...) Potential
Disulfide bond110 ↔ 121 By similarity
Disulfide bond139 ↔ 202 By similarity
Disulfide bond306 ↔ 315 By similarity

Natural variations

Alternative sequence86 – 10217TFVFT…QERLG → VTR in isoform 2.
VSP_042857
Natural variant3021R → C.
Corresponds to variant rs8192548 [ dbSNP | Ensembl ].
VAR_024467

Experimental info

Sequence conflict851Q → L in AAC51358. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 27, 2002. Version 2.
Checksum: 7CB847E7423DD0BC

FASTA32136,202
        10         20         30         40         50         60 
MQCRLPRGLA GALLTLLCMG LLCLRYHLNL SPQRVQGTPE LSQPNPGPPK LQLHDVFIAV 

        70         80         90        100        110        120 
KTTRAFHRLR LELLLDTWVS RTREQTFVFT DSPDKGLQER LGSHLVVTNC SAEHSHPALS 

       130        140        150        160        170        180 
CKMAAEFDTF LASGLRWFCH VDDDNYVNPR ALLQLLRAFP LARDVYVGRP SLNRPIHASE 

       190        200        210        220        230        240 
PQPHNRTRLV QFWFATGGAG FCINRKLALK MAPWASGSRF MDTSALIRLP DDCTMGYIIE 

       250        260        270        280        290        300 
CKLGGRLQPS PLFHSHLETL QLLRTAQLPE QVTLSYGVFE GKLNVIKLQG PFSPEEDPSR 

       310        320 
FRSLHCLLYP DTPWCPQLGA R 

« Hide

Isoform 2 [UniParc].

Checksum: 62DAF2173EA15DB6
Show »

FASTA30734,666

References

« Hide 'large scale' references
[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]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]"Fringe is a glycosyltransferase that modifies Notch."
Moloney D.J., Panin V.M., Johnston S.H., Chen J., Shao L., Wilson R., Wang Y., Stanley P., Irvine K.D., Haltiwanger R.S., Vogt T.F.
Nature 406:369-375(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Beta-1,3-N-acetylglucosaminyltransferase manic fringe

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS13947.1. [O00587-1]
CCDS54525.1. [O00587-2]
RefSeqNP_001159815.1. NM_001166343.1. [O00587-2]
NP_002396.2. NM_002405.3. [O00587-1]
UniGeneHs.517603.

3D structure databases

ProteinModelPortalO00587.
SMRO00587. Positions 50-318.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000349490.

Protein family/group databases

CAZyGT31. Glycosyltransferase Family 31.

Proteomic databases

PaxDbO00587.
PRIDEO00587.

Protocols and materials databases

DNASU4242.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356998; ENSP00000349490; ENSG00000100060. [O00587-1]
ENST00000416983; ENSP00000413855; ENSG00000100060. [O00587-2]
GeneID4242.
KEGGhsa:4242.
UCSCuc003ass.2. human. [O00587-1]
uc011anj.2. human. [O00587-2]

Organism-specific databases

CTD4242.
GeneCardsGC22M037865.
H-InvDBHIX0041190.
HGNCHGNC:7038. MFNG.
HPAHPA048936.
MIM602577. gene.
neXtProtNX_O00587.
PharmGKBPA30775.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG70217.
HOGENOMHOG000046678.
HOVERGENHBG007986.
InParanoidO00587.
KOK05948.
OMALRWFCHV.
OrthoDBEOG7ZSHTD.
PhylomeDBO00587.
TreeFamTF324207.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkO00587.

Gene expression databases

ArrayExpressO00587.
BgeeO00587.
CleanExHS_MFNG.
GenevestigatorO00587.

Family and domain databases

InterProIPR017374. Fringe.
IPR003378. Fringe-like.
[Graphical view]
PfamPF02434. Fringe. 1 hit.
[Graphical view]
PIRSFPIRSF038073. B-acetylgalactosaminyltfrase. 1 hit.
ProtoNetSearch...

Other

GeneWikiMFNG.
GenomeRNAi4242.
NextBio16729.
PROO00587.
SOURCESearch...

Entry information

Entry nameMFNG_HUMAN
AccessionPrimary (citable) accession number: O00587
Secondary accession number(s): B4DLT6, O43730, Q504S9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: March 27, 2002
Last modified: July 9, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM