O00587 (MFNG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	321 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Manganese Metal-binding
Molecular function	Developmental protein Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	pattern specification process Traceable author statement PubMed 9207795. Source: ProtInc positive regulation of Notch signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of protein binding Inferred from electronic annotation. Source: Compara
Cellular_component	extracellular space Traceable author statement Ref.1. Source: ProtInc integral to Golgi membrane Inferred from electronic annotation. Source: InterPro
Molecular_function	O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 321	321	Beta-1,3-N-acetylglucosaminyltransferase manic fringe		PRO_0000219182
Regions
	Topological domain	1 – 7	7	Cytoplasmic Potential
	Transmembrane	8 – 27	20	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	28 – 321	294	Lumenal Potential
Sites
	Active site	232	1	By similarity
	Metal binding	144	1	Manganese By similarity
	Metal binding	256	1	Manganese By similarity
	Binding site	70	1	Substrate By similarity
	Binding site	143	1	Substrate By similarity
Amino acid modifications
	Glycosylation	109	1	N-linked (GlcNAc...) Potential
	Glycosylation	185	1	N-linked (GlcNAc...) Potential
	Disulfide bond	110 ↔ 121		By similarity
	Disulfide bond	139 ↔ 202		By similarity
	Disulfide bond	306 ↔ 315		By similarity
Natural variations
	Alternative sequence	86 – 102	17	TFVFT…QERLG → VTR in isoform 2.		VSP_042857
	Natural variant	302	1	R → C. Corresponds to variant rs8192548 [ dbSNP | Ensembl ].		VAR_024467
Experimental info
	Sequence conflict	85	1	Q → L in AAC51358. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 27, 2002. Version 2. Checksum: 7CB847E7423DD0BC	FASTA	321	36,202
	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
	Isoform 2 [UniParc]. Checksum: 62DAF2173EA15DB6	FASTA	307	34,666
	10 20 30 40 50 60 MQCRLPRGLA GALLTLLCMG LLCLRYHLNL SPQRVQGTPE LSQPNPGPPK LQLHDVFIAV 70 80 90 100 110 120 KTTRAFHRLR LELLLDTWVS RTREQVTRSH LVVTNCSAEH SHPALSCKMA AEFDTFLASG 130 140 150 160 170 180 LRWFCHVDDD NYVNPRALLQ LLRAFPLARD VYVGRPSLNR PIHASEPQPH NRTRLVQFWF 190 200 210 220 230 240 ATGGAGFCIN RKLALKMAPW ASGSRFMDTS ALIRLPDDCT MGYIIECKLG GRLQPSPLFH 250 260 270 280 290 300 SHLETLQLLR TAQLPEQVTL SYGVFEGKLN VIKLQGPFSP EEDPSRFRSL HCLLYPDTPW CPQLGAR

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.
IPI	IPI00025339. IPI00798181.
RefSeq	NP_001159815.1. NM_001166343.1. NP_002396.2. NM_002405.3.
UniGene	Hs.517603.
3D structure databases
ProteinModelPortal	O00587.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000349490.
Protein family/group databases
CAZy	GT31. Glycosyltransferase Family 31.
Proteomic databases
PaxDb	O00587.
PRIDE	O00587.
Protocols and materials databases
DNASU	4242.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000356998; ENSP00000349490; ENSG00000100060. ENST00000416983; ENSP00000413855; ENSG00000100060.
GeneID	4242.
KEGG	hsa:4242.
UCSC	uc003ass.2. human.
Organism-specific databases
CTD	4242.
GeneCards	GC22M037865.
H-InvDB	HIX0041190.
HGNC	HGNC:7038. MFNG.
HPA	HPA048936.
MIM	602577. gene.
neXtProt	NX_O00587.
PharmGKB	PA30775.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG70217.
HOGENOM	HOG000046678.
HOVERGEN	HBG007986.
InParanoid	O00587.
KO	K05948.
OMA	LRWFCHV.
OrthoDB	EOG4GQQ57.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction.
Gene expression databases
ArrayExpress	O00587.
Bgee	O00587.
CleanEx	HS_MFNG.
Genevestigator	O00587.
GermOnline	ENSG00000100060. Homo sapiens.
Family and domain databases
InterPro	IPR017374. Fringe. IPR003378. Fringe-like. [Graphical view]
Pfam	PF02434. Fringe. 1 hit. [Graphical view]
PIRSF	PIRSF038073. B-acetylgalactosaminyltfrase. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	4242.
NextBio	16729.
SOURCE	Search...

Entry information

Entry name

MFNG_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.