Q8WZA1 (PMGT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1
Short name=POMGnT1
EC=2.4.1.-

Alternative name(s):
UDP-GlcNAc:alpha-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I.2
Short name=GnT I.2

Gene names

Name:	POMGNT1
Synonyms:	MGAT1.2
ORF Names:	UNQ746/PRO1475

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	660 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Participates in O-mannosyl glycosylation. May be responsible for the synthesis of the GlcNAc(beta1-2)Man(alpha1-)O-Ser/Thr moiety on alpha-dystroglycan and other O-mannosylated proteins. Is specific for alpha linked terminal mannose and does not have MGAT3, MGAT4, MGAT5, MGAT7 or MGAT8 activity.
Catalytic activity	UDP-N-acetyl-D-glucosamine + Man-R = N-acetyl-D-glucosamine-beta-1,2-Man-R + UDP.
Cofactor	Manganese.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein Potential.
Tissue specificity	Constitutively expressed. An additional weaker band is also detected in spinal cord, lymph node, and trachea. Expressed especially in astrocytes. Also expressed in immature and mature neurons. Ref.1 Ref.8
Domain	Amino acid residues between 299-311 are important for both protein expression and enzymatic activity. The minimal catalytic domain is located between positions 299-651. Single amino acid substitutions in the stem domain from MEB patients abolished the activity of the membrane-bound form but not the soluble form. This suggests that the stem domain of the soluble form is unnecessary for activity, but that some amino acids play a crucial role in the membrane-bound form. Ref.11
Involvement in disease	Muscular dystrophy-dystroglycanopathy congenital with brain and eye anomalies A3 (MDDGA3) [MIM:253280]: An autosomal recessive disorder characterized by congenital muscular dystrophy, ocular abnormalities, cobblestone lissencephaly, and cerebellar and pontine hypoplasia. Patients present severe congenital myopia, congenital glaucoma, pallor of the optic disks, retinal hypoplasia, mental retardation, hydrocephalus, abnormal electroencephalograms, generalized muscle weakness and myoclonic jerks. Included diseases are the more severe Walker-Warburg syndrome and the slightly less severe muscle-eye-brain disease. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.2 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Muscular dystrophy-dystroglycanopathy congenital with mental retardation B3 (MDDGB3) [MIM:613151]: An autosomal recessive disorder characterized by congenital muscular dystrophy associated with mental retardation and mild structural brain abnormalities. Clinical features include mental retardation, white matter changes, cerebellar cysts, pontine hypoplasia, myopia, optic atrophy, decreased alpha-dystroglycan on muscle biopsy and increased serum creatine kinase. Note: The disease is caused by mutations affecting the gene represented in this entry. Muscular dystrophy-dystroglycanopathy limb-girdle C3 (MDDGC3) [MIM:613157]: A rare form of limb-girdle muscular dystrophy with normal cognition. Muscle biopsy shows dystrophic changes with variable staining for glycosylated alpha-dystroglycan. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16
Sequence similarities	Belongs to the glycosyltransferase 13 family.
Biophysicochemical properties	Kinetic parameters: KM=1.85 mM for mannosylpeptide Ref.1 Ref.8 KM=0.73 mM for UDP-GlcNAc KM=30 mM for Man(alpha1-)O-benzyl KM=12 mM for CYA[Man(alpha1-)O-T]AV pH dependence: Optimum pH is 6.0.
Sequence caution	The sequence BAB14207.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Polymorphism
Disease	Congenital muscular dystrophy Disease mutation Limb-girdle muscular dystrophy Lissencephaly
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Manganese
Molecular function	Glycosyltransferase Transferase
PTM	Isopeptide bond Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein O-linked glycosylation Inferred from direct assay Ref.1. Source: MGI
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity Inferred from direct assay Ref.8. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 660	660	Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1		PRO_0000191390
Regions
	Topological domain	1 – 37	37	Cytoplasmic Potential
	Transmembrane	38 – 58	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	59 – 660	602	Lumenal Potential
	Compositional bias	263 – 267	5	Poly-Arg
Amino acid modifications
	Cross-link	537		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9
	Cross-link	538		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9
Natural variations
	Natural variant	176	1	T → P in MDDGA3. Ref.15		VAR_065021
	Natural variant	198	1	S → R in MDDGA3. Ref.14		VAR_065022
	Natural variant	223	1	E → K in MDDGA3; specific activity abolished in the membrane bound form but not the soluble form. Ref.2 Ref.10 Ref.11		VAR_023101
	Natural variant	250	1	E → V. Ref.7 Corresponds to variant rs17855359 [ dbSNP | Ensembl ].		VAR_030645
	Natural variant	265	1	R → H in MDDGA3; found on the same allele as Q-311; unknown pathological significance. Ref.12		VAR_023102
	Natural variant	269	1	C → Y in MDDGA3; specific activity abolished of the membrane bound form but not the soluble form. Ref.2 Ref.10 Ref.11		VAR_023103
	Natural variant	311	1	R → Q in MDDGA3 and MDDGB3. Ref.12 Ref.14		VAR_023104
	Natural variant	367	1	R → H in MDDGA3. Ref.15		VAR_065023
	Natural variant	425	1	W → S in MDDGA3. Ref.13		VAR_023105
	Natural variant	427	1	D → H in MDDGA3. Ref.15		VAR_065024
	Natural variant	442	1	R → C in MDDGA3. Ref.12 Corresponds to variant rs28940869 [ dbSNP | Ensembl ].		VAR_023106
	Natural variant	490	1	C → Y in MDDGA3 and MDDGB3. Ref.13 Ref.14 Ref.15		VAR_023107
	Natural variant	493	1	P → R in MDDGA3; specific activity abolished. Ref.1 Ref.10 Corresponds to variant rs28942068 [ dbSNP | Ensembl ].		VAR_023108
	Natural variant	504	1	V → I. Corresponds to variant rs17102066 [ dbSNP | Ensembl ].		VAR_030646
	Natural variant	550	1	S → N in MDDGA3. Ref.1		VAR_023109
	Natural variant	556	1	D → N in MDDGC3; normal enzyme activity but altered kinetic properties. Ref.16		VAR_065025
	Natural variant	605	1	R → P in MDDGB3. Ref.17		VAR_065026
	Natural variant	623	1	M → V. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6 Ref.7 Ref.8 Corresponds to variant rs6659553 [ dbSNP | Ensembl ].		VAR_023110
Experimental info
	Sequence conflict	636	1	P → L in BAA91053. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q8WZA1 [UniParc]. Last modified November 2, 2010. Version 2. Checksum: C58D0E543E033F17	FASTA	660	75,252
	10 20 30 40 50 60 MDDWKPSPLI KPFGARKKRS WYLTWKYKLT NQRALRRFCQ TGAVLFLLVT VIVNIKLILD 70 80 90 100 110 120 TRRAISEANE DPEPEQDYDE ALGRLEPPRR RGSGPRRVLD VEVYSSRSKV YVAVDGTTVL 130 140 150 160 170 180 EDEAREQGRG IHVIVLNQAT GHVMAKRVFD TYSPHEDEAM VLFLNMVAPG RVLICTVKDE 190 200 210 220 230 240 GSFHLKDTAK ALLRSLGSQA GPALGWRDTW AFVGRKGGPV FGEKHSKSPA LSSWGDPVLL 250 260 270 280 290 300 KTDVPLSSAE EAECHWADTE LNRRRRRFCS KVEGYGSVCS CKDPTPIEFS PDPLPDNKVL 310 320 330 340 350 360 NVPVAVIAGN RPNYLYRMLR SLLSAQGVSP QMITVFIDGY YEEPMDVVAL FGLRGIQHTP 370 380 390 400 410 420 ISIKNARVSQ HYKASLTATF NLFPEAKFAV VLEEDLDIAV DFFSFLSQSI HLLEEDDSLY 430 440 450 460 470 480 CISAWNDQGY EHTAEDPALL YRVETMPGLG WVLRRSLYKE ELEPKWPTPE KLWDWDMWMR 490 500 510 520 530 540 MPEQRRGREC IIPDVSRSYH FGIVGLNMNG YFHEAYFKKH KFNTVPGVQL RNVDSLKKEA 550 560 570 580 590 600 YEVEVHRLLS EAEVLDHSKN PCEDSFLPDT EGHTYVAFIR MEKDDDFTTW TQLAKCLHIW 610 620 630 640 650 660 DLDVRGNHRG LWRLFRKKNH FLMVGVPASP YSVKKPPSVT PIFLEPPPKE EGAPGAPEQT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Muscular dystrophy and neuronal migration disorder caused by mutations in a glycosyltransferase, POMGnT1." Yoshida A., Kobayashi K., Manya H., Taniguchi K., Kano H., Mizuno M., Inazu T., Mitsuhashi H., Takahashi S., Takeuchi M., Herrmann R., Straub V., Talim B., Voit T., Topaloglu H., Toda T., Endo T. Dev. Cell 1:717-724(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, VARIANTS MDDGA3 ARG-493 AND ASN-550, VARIANT VAL-623. Tissue: Brain.
[2]	"Worldwide distribution and broader clinical spectrum of muscle-eye-brain disease." Taniguchi K., Kobayashi K., Saito K., Yamanouchi H., Ohnuma A., Hayashi Y.K., Manya H., Jin D.K., Lee M., Parano E., Falsaperla R., Pavone P., Coster R.V., Talim B., Steinbrecher A., Straub V., Nishino I., Topaloglu H. , Voit T., Endo T., Toda T. Hum. Mol. Genet. 12:527-534(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS MDDGA3 LYS-223 AND TYR-269, VARIANT VAL-623. Tissue: Brain.
[3]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-623.
[4]	"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], VARIANT VAL-623.
[5]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-623.
[7]	"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], VARIANTS VAL-250 AND VAL-623. Tissue: Placenta.
[8]	"Cloning and expression of a novel UDP-GlcNAc:alpha-D-mannoside beta-1,2-N-acetylglucosaminyltransferase homologous to UDP-GlcNAc:alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I." Zhang W., Betel D., Schachter H. Biochem. J. 361:153-162(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 84-660, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, VARIANT VAL-623. Tissue: Brain.
[9]	"Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry." Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D. Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-537 AND LYS-538, MASS SPECTROMETRY. Tissue: Mammary cancer.
[10]	"Loss-of-function of an N-acetylglucosaminyltransferase, POMGnT1, in muscle-eye-brain disease." Manya H., Sakai K., Kobayashi K., Taniguchi K., Kawakita M., Toda T., Endo T. Biochem. Biophys. Res. Commun. 306:93-97(2003) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS MDDGA3 LYS-223; TYR-269 AND ARG-493.
[11]	"Structure-function analysis of human protein O-linked mannose beta1,2-N-acetylglucosaminyltransferase 1, POMGnT1." Akasaka-Manya K., Manya H., Kobayashi K., Toda T., Endo T. Biochem. Biophys. Res. Commun. 320:39-44(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION OF CATALYTIC DOMAIN, CHARACTERIZATION OF VARIANTS MDDGA3 LYS-223 AND TYR-269.
[12]	"POMGnT1 gene alterations in a family with neurological abnormalities." Vervoort V.S., Holden K.R., Ukadike K.C., Collins J.S., Saul R.A., Srivastava A.K. Ann. Neurol. 56:143-148(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MDDGA3 HIS-265; GLN-311 AND CYS-442.
[13]	"POMGnT1 mutation and phenotypic spectrum in muscle-eye-brain disease." Diesen C., Saarinen A., Pihko H., Rosenlew C., Cormand B., Dobyns W.B., Dieguez J., Valanne L., Joensuu T., Lehesjoki A.-E. J. Med. Genet. 41:E115-E115(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MDDGA3 SER-425 AND TYR-490.
[14]	"POMGnT1 mutations in congenital muscular dystrophy: genotype-phenotype correlation and expanded clinical spectrum." Biancheri R., Bertini E., Falace A., Pedemonte M., Rossi A., D'Amico A., Scapolan S., Bergamino L., Petrini S., Cassandrini D., Broda P., Manfredi M., Zara F., Santorelli F.M., Minetti C., Bruno C. Arch. Neurol. 63:1491-1495(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MDDGA3 ARG-198 AND TYR-490, VARIANT MDDGB3 GLN-311.
[15]	"Brain involvement in muscular dystrophies with defective dystroglycan glycosylation." Clement E., Mercuri E., Godfrey C., Smith J., Robb S., Kinali M., Straub V., Bushby K., Manzur A., Talim B., Cowan F., Quinlivan R., Klein A., Longman C., McWilliam R., Topaloglu H., Mein R., Abbs S. , North K., Barkovich A.J., Rutherford M., Muntoni F. Ann. Neurol. 64:573-582(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MDDGA3 PRO-176; HIS-367 AND HIS-427, VARIANT MDDGB3 TYR-490.
[16]	"Mild POMGnT1 mutations underlie a novel limb-girdle muscular dystrophy variant." Clement E.M., Godfrey C., Tan J., Brockington M., Torelli S., Feng L., Brown S.C., Jimenez-Mallebrera C., Sewry C.A., Longman C., Mein R., Abbs S., Vajsar J., Schachter H., Muntoni F. Arch. Neurol. 65:137-141(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MDDGC3 ASN-556, CHARACTERIZATION OF VARIANT MDDGC3 ASN-556.
[17]	"Congenital muscular dystrophies with defective glycosylation of dystroglycan: a population study." Mercuri E., Messina S., Bruno C., Mora M., Pegoraro E., Comi G.P., D'Amico A., Aiello C., Biancheri R., Berardinelli A., Boffi P., Cassandrini D., Laverda A., Moggio M., Morandi L., Moroni I., Pane M., Pezzani R. , Pichiecchio A., Pini A., Minetti C., Mongini T., Mottarelli E., Ricci E., Ruggieri A., Saredi S., Scuderi C., Tessa A., Toscano A., Tortorella G., Trevisan C.P., Uggetti C., Vasco G., Santorelli F.M., Bertini E. Neurology 72:1802-1809(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MDDGB3 PRO-605.
+	Additional computationally mapped references.

Web resources

GeneReviews

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB057356 mRNA. Translation: BAB71960.1. AY358592 mRNA. Translation: AAQ88955.1. AK000284 mRNA. Translation: BAA91053.1. AK022727 mRNA. Translation: BAB14207.1. Different initiation. AL672043 Genomic DNA. Translation: CAH72470.1. CH471059 Genomic DNA. Translation: EAX06932.1. CH471059 Genomic DNA. Translation: EAX06933.1. CH471059 Genomic DNA. Translation: EAX06935.1. BC001471 mRNA. Translation: AAH01471.1. AF250859 mRNA. Translation: AAF71270.2.
IPI	IPI00550558.
RefSeq	NP_060209.3. NM_017739.3.
UniGene	Hs.525134.
3D structure databases
ProteinModelPortal	Q8WZA1.
SMR	Q8WZA1. Positions 302-542.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8WZA1. 4 interactions.
STRING	9606.ENSP00000361052.
Protein family/group databases
CAZy	GT13. Glycosyltransferase Family 13.
PTM databases
PhosphoSite	Q8WZA1.
Polymorphism databases
DMDM	311033411.
Proteomic databases
PaxDb	Q8WZA1.
PRIDE	Q8WZA1.
Protocols and materials databases
DNASU	55624.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000371984; ENSP00000361052; ENSG00000085998.
GeneID	55624.
KEGG	hsa:55624.
UCSC	uc001cpe.3. human.
Organism-specific databases
CTD	55624.
GeneCards	GC01M046654.
HGNC	HGNC:19139. POMGNT1.
HPA	HPA044518.
MIM	253280. phenotype. 606822. gene. 613151. phenotype. 613157. phenotype.
neXtProt	NX_Q8WZA1.
Orphanet	588. Muscle eye brain disease. 899. Walker-Warburg syndrome.
PharmGKB	PA142671161.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG148227.
HOVERGEN	HBG055279.
KO	K09666.
OrthoDB	EOG4FTW03.
PhylomeDB	Q8WZA1.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	Q8WZA1.
Bgee	Q8WZA1.
CleanEx	HS_POMGNT1.
Genevestigator	Q8WZA1.
GermOnline	ENSG00000085998. Homo sapiens.
Family and domain databases
InterPro	IPR004139. Glyco_trans_13. [Graphical view]
PANTHER	PTHR10468. PTHR10468. 1 hit.
Pfam	PF03071. GNT-I. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	POMGNT1. human.
GenomeRNAi	55624.
NextBio	60240.
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Entry information

Entry name

PMGT1_HUMAN

Accession

Primary (citable) accession number: Q8WZA1
Secondary accession number(s): D3DQ16 , Q5VST2, Q9BV55, Q9H9L8, Q9NXF9, Q9NYF7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	November 2, 2010
Last modified:	May 1, 2013
This is version 97 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.