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Q91X88 (PMGT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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.-
Gene names
Name:Pomgnt1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length660 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

Catalytic activity

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

Cofactor

Manganese By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein Potential.

Developmental stage

Broadly expressed in late embryonic and early postnatal cerebellar neurons, including premigratory granule neurons of the external granule cell layer. Expression is maintained in neurons of the internal granule cell layer after migration is complete. Expressed in Purkinje cells throughout development. Expressed in Bergmann glial scaffolds used by granule cells during early posnatal radial migration. Ref.5

Sequence similarities

Belongs to the glycosyltransferase 13 family.

Ontologies

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q91X88-1)

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: Q91X88-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-22: Missing.
     23-40: LTWKYKLTNQRALRRFCQ → MEGTKEVKDSNGKIQDHG
Isoform 3 (identifier: Q91X88-3)

The sequence of this isoform differs from the canonical sequence as follows:
     218-250: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 660660Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1
PRO_0000191391

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) By similarity
Cross-link538Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Alternative sequence1 – 2222Missing in isoform 2.
VSP_014972
Alternative sequence23 – 4018LTWKY…RRFCQ → MEGTKEVKDSNGKIQDHG in isoform 2.
VSP_014973
Alternative sequence218 – 25033Missing in isoform 3.
VSP_014974

Experimental info

Sequence conflict4241A → S in BAB29863. Ref.2
Sequence conflict5571H → P in BAB22251. Ref.2

Sequences

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

Last modified December 1, 2001. Version 1.
Checksum: 4DE09765C0F3EF7C

FASTA66075,110
        10         20         30         40         50         60 
MDDWKPSPLI KPFGARKKRS WYLTWKYKLT NQRALRRFCQ TGAVLFLLVT VIVNIKLILD 

        70         80         90        100        110        120 
TRRAISEANE DPEPEQDYDE ALGRLESPRR RGSSPRRVLD VEVYSSRSKV YVAVDGTTVL 

       130        140        150        160        170        180 
EDEAREQGRG IHVIVLNQAT GHVMAKRVFD TYSPHEDEAM VLFLNMVAPG RVLICTVKDE 

       190        200        210        220        230        240 
GSFHLKDTAK ALLRSLGSQA GPALGWRDTW AFVGRKGGPV LGEKHSKSPA 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 WVLRKSLYKE ELEPKWPTPE KLWDWDMWMR 

       490        500        510        520        530        540 
MPEQRRGREC IIPDVSRSYH FGIVGLNMNG YFHEAYFKKH KFNTVPGVQL RNVDSLKKEA 

       550        560        570        580        590        600 
YEVEIHRLLS EAEVLDHSKD PCEDSFLPDT EGHTYVAFIR METDDDFATW TQLAKCLHIW 

       610        620        630        640        650        660 
DLDVRGNHRG LWRLFRKKNH FLVVGVPASP YSVKKPPSVT PIFLEPPPKE EGAPGAAEQT 

« Hide

Isoform 2 [UniParc].

Checksum: A8656C7EA33D2767
Show »

FASTA63872,068
Isoform 3 [UniParc].

Checksum: 334E4F56BC5D342B
Show »

FASTA62771,725

References

« Hide 'large scale' references
[1]Minowa M.T., Yoshida A., Endo T., Takeuchi M.
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
Strain: 129/SvJ.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
Strain: C57BL/6J.
Tissue: Kidney and Testis.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"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).
Strain: FVB/N.
Tissue: Salivary gland.
[5]"Expression of dystroglycan, fukutin and POMGnT1 during mouse cerebellar development."
Henion T.R., Qu Q., Smith F.I.
Brain Res. Mol. Brain Res. 112:177-181(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB053220 mRNA. Translation: BAC55021.1.
AB053221 Genomic DNA. Translation: BAC55022.1.
AK002638 mRNA. Translation: BAB22251.1.
AK019640 mRNA. Translation: BAB31822.1.
AK015478 mRNA. Translation: BAB29863.1.
AL611947 Genomic DNA. Translation: CAM20673.1.
BC011201 mRNA. Translation: AAH11201.1.
RefSeqNP_080927.1. NM_026651.2.
NP_084062.2. NM_029786.2.
XP_006503414.1. XM_006503351.1.
UniGeneMm.196045.

3D structure databases

ProteinModelPortalQ91X88.
SMRQ91X88. Positions 83-250, 302-542.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGT13. Glycosyltransferase Family 13.

PTM databases

PhosphoSiteQ91X88.

Proteomic databases

PRIDEQ91X88.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000106494; ENSMUSP00000102103; ENSMUSG00000028700. [Q91X88-2]
ENSMUST00000106496; ENSMUSP00000102105; ENSMUSG00000028700. [Q91X88-3]
ENSMUST00000106498; ENSMUSP00000102107; ENSMUSG00000028700. [Q91X88-1]
ENSMUST00000120083; ENSMUSP00000112751; ENSMUSG00000028700. [Q91X88-1]
ENSMUST00000121052; ENSMUSP00000112911; ENSMUSG00000028700. [Q91X88-1]
GeneID68273.
KEGGmmu:68273.
UCSCuc008ugh.2. mouse. [Q91X88-1]

Organism-specific databases

CTD55624.
MGIMGI:1915523. Pomgnt1.

Phylogenomic databases

eggNOGNOG148227.
GeneTreeENSGT00530000063632.
HOGENOMHOG000231121.
HOVERGENHBG055279.
InParanoidA2A8F8.
KOK09666.
OMANHFLVVG.
OrthoDBEOG786H2N.
PhylomeDBQ91X88.
TreeFamTF320555.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

BgeeQ91X88.
GenevestigatorQ91X88.

Family and domain databases

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

Other

ChiTaRSPOMGNT1. mouse.
NextBio326888.
PROQ91X88.
SOURCESearch...

Entry information

Entry namePMGT1_MOUSE
AccessionPrimary (citable) accession number: Q91X88
Secondary accession number(s): A2A8F8 expand/collapse secondary AC list , Q9D2H7, Q9D5D3, Q9DCN3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot