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Q8WZA1 (PMGT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length660 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Ref.1

Catalytic activity

UDP-N-acetyl-alpha-D-glucosamine + O-alpha-D-mannosylprotein = UDP + N-acetyl-beta-D-glucosaminyl-(1->2)-O-alpha-D-mannosylprotein. Ref.1

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.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8WZA1-1)

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: Q8WZA1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     624-660: VGVPASPYSV...EGAPGAPEQT → SEEATLSHPN...LLFVQISKAG
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 660660Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1
PRO_0000191390

Regions

Topological domain1 – 3737Cytoplasmic Potential
Transmembrane38 – 5821Helical; Signal-anchor for type II membrane protein; Potential
Topological domain59 – 660602Lumenal Potential
Compositional bias263 – 2675Poly-Arg

Amino acid modifications

Cross-link537Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9
Cross-link538Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9

Natural variations

Alternative sequence624 – 66037VGVPA…APEQT → SEEATLSHPNFPGATPKGGG SPRSPRTDMRPPPGPCGAGP GSESNLFIDCPEGLENRPNL EGLDFFLGWNAALRVGLALT QETAVPNPWTGPAGAHMLTQ THSETLRHWTRPPLSLLFVQ ISKAG in isoform 2.
VSP_054029
Natural variant1761T → P in MDDGA3. Ref.15
VAR_065021
Natural variant1981S → R in MDDGA3. Ref.14
VAR_065022
Natural variant2231E → 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 variant2501E → V. Ref.7
Corresponds to variant rs17855359 [ dbSNP | Ensembl ].
VAR_030645
Natural variant2651R → H in MDDGA3; found on the same allele as Q-311; unknown pathological significance. Ref.12
VAR_023102
Natural variant2691C → 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 variant3111R → Q in MDDGA3 and MDDGB3. Ref.12 Ref.14
VAR_023104
Natural variant3671R → H in MDDGA3. Ref.15
VAR_065023
Natural variant4251W → S in MDDGA3. Ref.13
VAR_023105
Natural variant4271D → H in MDDGA3. Ref.15
VAR_065024
Natural variant4421R → C in MDDGA3. Ref.12
Corresponds to variant rs28940869 [ dbSNP | Ensembl ].
VAR_023106
Natural variant4901C → Y in MDDGA3 and MDDGB3. Ref.13 Ref.14 Ref.15
VAR_023107
Natural variant4931P → R in MDDGA3; specific activity abolished. Ref.1 Ref.10
Corresponds to variant rs28942068 [ dbSNP | Ensembl ].
VAR_023108
Natural variant5041V → I.
Corresponds to variant rs17102066 [ dbSNP | Ensembl ].
VAR_030646
Natural variant5501S → N in MDDGA3. Ref.1
VAR_023109
Natural variant5561D → N in MDDGC3; normal enzyme activity but altered kinetic properties. Ref.16
Corresponds to variant rs74374973 [ dbSNP | Ensembl ].
VAR_065025
Natural variant6051R → P in MDDGB3. Ref.17
VAR_065026
Natural variant6231M → 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 conflict6361P → L in BAA91053. Ref.3
Isoform 2:
Sequence conflict6361G → K in AK056186. Ref.4

Sequences

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

Last modified November 2, 2010. Version 2.
Checksum: C58D0E543E033F17

FASTA66075,252
        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 

« Hide

Isoform 2 [UniParc].

Checksum: B88BFD957237FEFD
Show »

FASTA74884,700

References

« Hide '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] (ISOFORM 1), TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, VARIANTS MDDGA3 ARG-493 AND ASN-550, VARIANT VAL-623, FUNCTION, CATALYTIC ACTIVITY.
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. expand/collapse author list , Voit T., Endo T., Toda T.
Hum. Mol. Genet. 12:527-534(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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. expand/collapse author list , 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] (ISOFORM 1), 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. 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] (ISOFORMS 1 AND 2), 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. expand/collapse author list , 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. expand/collapse author list , 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] (ISOFORM 1), 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 (ISOFORM 1), 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.
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. expand/collapse author list , 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. expand/collapse author list , 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.
AK056186 mRNA. No translation available.
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.
RefSeqNP_060209.3. NM_017739.3.
UniGeneHs.525134.

3D structure databases

ProteinModelPortalQ8WZA1.
SMRQ8WZA1. Positions 94-250, 302-542.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120763. 5 interactions.
IntActQ8WZA1. 4 interactions.
STRING9606.ENSP00000361052.

Chemistry

ChEMBLCHEMBL2321629.

Protein family/group databases

CAZyGT13. Glycosyltransferase Family 13.

PTM databases

PhosphoSiteQ8WZA1.

Polymorphism databases

DMDM311033411.

Proteomic databases

PaxDbQ8WZA1.
PRIDEQ8WZA1.

Protocols and materials databases

DNASU55624.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371984; ENSP00000361052; ENSG00000085998.
ENST00000371986; ENSP00000361054; ENSG00000085998.
ENST00000371992; ENSP00000361060; ENSG00000085998.
GeneID55624.
KEGGhsa:55624.
UCSCuc001cpe.3. human.

Organism-specific databases

CTD55624.
GeneCardsGC01M046654.
HGNCHGNC:19139. POMGNT1.
HPAHPA044518.
MIM253280. phenotype.
606822. gene.
613151. phenotype.
613157. phenotype.
neXtProtNX_Q8WZA1.
Orphanet206564. Autosomal recessive limb-girdle muscular dystrophy type 2O.
370959. Congenital muscular dystrophy with cerebellar involvement.
588. Muscle-eye-brain disease.
899. Walker-Warburg syndrome.
PharmGKBPA142671161.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG148227.
HOGENOMHOG000231121.
HOVERGENHBG055279.
KOK09666.
OMANHFLVVG.
OrthoDBEOG786H2N.
PhylomeDBQ8WZA1.
TreeFamTF320555.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ8WZA1.
BgeeQ8WZA1.
CleanExHS_POMGNT1.
GenevestigatorQ8WZA1.

Family and domain databases

InterProIPR004139. Glyco_trans_13.
[Graphical view]
PANTHERPTHR10468. PTHR10468. 1 hit.
PfamPF03071. GNT-I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPOMGNT1. human.
GeneWikiPOMGNT1.
GenomeRNAi55624.
NextBio60240.
PROQ8WZA1.
SOURCESearch...

Entry information

Entry namePMGT1_HUMAN
AccessionPrimary (citable) accession number: Q8WZA1
Secondary accession number(s): D3DQ16 expand/collapse secondary AC list , Q5VST2, Q5VST3, Q9BV55, Q9H9L8, Q9NXF9, Q9NYF7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: November 2, 2010
Last modified: April 16, 2014
This is version 108 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

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 1

Human chromosome 1: entries, gene names and cross-references to MIM