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Q9Y6A1 (POMT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. 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-mannosyl-transferase 1

EC=2.4.1.109
Alternative name(s):
Dolichyl-phosphate-mannose--protein mannosyltransferase 1
Gene names
Name:POMT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length747 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient. Ref.7 Ref.8

Catalytic activity

Dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein. Ref.8

Enzyme regulation

Slightly activated by Mg2+ and inhibited by both Ca+ and Mn2+. EDTA ha no effect on activity in vitro. Ref.8

Pathway

Protein modification; protein glycosylation.

Subunit structure

Interacts with POMT2 Probable.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.8.

Tissue specificity

Widely expressed. Highly expressed in testis, heart and pancreas. Detected at lower levels in kidney, skeletal muscle, brain, placenta, lung and liver.

Involvement in disease

Muscular dystrophy-dystroglycanopathy congenital with mental retardation B1 (MDDGB1) [MIM:613155]: An autosomal recessive disorder characterized by congenital muscular dystrophy associated with mental retardation and mild structural brain abnormalities.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13 Ref.14 Ref.15

Muscular dystrophy-dystroglycanopathy congenital with brain and eye anomalies A1 (MDDGA1) [MIM:236670]: An autosomal recessive disorder characterized by congenital muscular dystrophy associated with cobblestone lissencephaly and other brain anomalies, eye malformations, profound mental retardation, and death usually in the first years of life. 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.

Muscular dystrophy-dystroglycanopathy limb-girdle C1 (MDDGC1) [MIM:609308]: An autosomal recessive degenerative myopathy associated with mild mental retardation without any obvious structural brain abnormality. An abnormal alpha-dystroglycan pattern in observed in the muscle.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12

Sequence similarities

Belongs to the glycosyltransferase 39 family.

Contains 3 MIR domains.

Sequence caution

The sequence BAA91135.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAA91190.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCongenital muscular dystrophy
Disease mutation
Dystroglycanopathy
Limb-girdle muscular dystrophy
Lissencephaly
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandMetal-binding
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement Ref.1. Source: ProtInc

extracellular matrix organization

Inferred from electronic annotation. Source: Ensembl

mannosylation

Traceable author statement Ref.1. Source: GOC

multicellular organismal development

Traceable author statement Ref.1. Source: ProtInc

protein O-linked glycosylation

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentacrosomal vesicle

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Traceable author statement Ref.1. Source: ProtInc

endoplasmic reticulum membrane

Inferred from direct assay Ref.8. Source: UniProtKB

integral component of membrane

Traceable author statement Ref.1. Source: ProtInc

sarcoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

   Molecular_functiondolichyl-phosphate-mannose-protein mannosyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

mannosyltransferase activity

Traceable author statement Ref.1. Source: ProtInc

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q9Y6A1-1)

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: Q9Y6A1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     234-255: Missing.
Isoform 3 (identifier: Q9Y6A1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-54: Missing.
     234-255: Missing.
Isoform 4 (identifier: Q9Y6A1-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-117: Missing.
     234-255: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 747747Protein O-mannosyl-transferase 1
PRO_0000121484

Regions

Transmembrane8 – 2821Helical; Potential
Transmembrane40 – 6021Helical; Potential
Transmembrane68 – 8821Helical; Potential
Transmembrane99 – 11921Helical; Potential
Transmembrane122 – 14221Helical; Potential
Transmembrane154 – 17421Helical; Potential
Transmembrane183 – 20321Helical; Potential
Transmembrane206 – 22621Helical; Potential
Transmembrane269 – 28921Helical; Potential
Transmembrane597 – 61721Helical; Potential
Transmembrane636 – 65621Helical; Potential
Transmembrane661 – 68121Helical; Potential
Domain318 – 38164MIR 1
Domain392 – 44958MIR 2
Domain453 – 51361MIR 3

Amino acid modifications

Glycosylation4351N-linked (GlcNAc...) Potential
Glycosylation4711N-linked (GlcNAc...) Ref.9
Glycosylation5391N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 117117Missing in isoform 4.
VSP_041024
Alternative sequence1 – 5454Missing in isoform 3.
VSP_007590
Alternative sequence234 – 25522Missing in isoform 2, isoform 3 and isoform 4.
VSP_007591
Natural variant651G → R in MDDGB1. Ref.13 Ref.14 Ref.15
VAR_065027
Natural variant761G → R in MDDGA1. Ref.7
Corresponds to variant rs28941782 [ dbSNP | Ensembl ].
VAR_015734
Natural variant1051R → C in MDDGA1; severe Walker-Warburg syndrome. Ref.13
VAR_065028
Natural variant1051R → H in MDDGA1; severe Walker-Warburg syndrome. Ref.13
VAR_065029
Natural variant1401Missing in MDDGB1. Ref.13
VAR_065030
Natural variant2001A → P in MDDGC1; a common founder mutation. Ref.12
VAR_022661
Natural variant2071G → V in MDDGA1; severe Walker-Warburg syndrome. Ref.13
VAR_065031
Natural variant2511Q → R. Ref.1 Ref.2
Corresponds to variant rs2296949 [ dbSNP | Ensembl ].
VAR_034390
Natural variant2511Q → W Requires 2 nucleotide substitutions.
Corresponds to variant rs3887873 [ dbSNP | Ensembl ].
VAR_034389
Natural variant2851L → F. Ref.13
VAR_065032
Natural variant3271V → I.
Corresponds to variant rs4740164 [ dbSNP | Ensembl ].
VAR_034391
Natural variant4211Missing in MDDGA1; associated with the loss of function of alpha dystroglycan as a matrix receptor. Ref.10
VAR_022662
Natural variant4281V → D in MDDGA1. Ref.7
VAR_015735
Natural variant4331D → E.
Corresponds to variant rs11243406 [ dbSNP | Ensembl ].
VAR_034392
Natural variant5221R → K. Ref.13
Corresponds to variant rs117985576 [ dbSNP | Ensembl ].
VAR_065033
Natural variant5371S → R in MDDGA1 and MDDGB1. Ref.11 Ref.15
Corresponds to variant rs150367385 [ dbSNP | Ensembl ].
VAR_026697
Natural variant5821W → C in MDDGB1. Ref.13
VAR_065034
Natural variant5901Q → H in MDDGB1. Ref.13 Ref.14
VAR_065035
Natural variant6691A → T in MDDGB1. Ref.14
VAR_065036

Experimental info

Sequence conflict371P → Q in AAH22877. Ref.6
Sequence conflict1431E → K in AAD41245. Ref.1
Sequence conflict1471I → V in BAG58462. Ref.2
Sequence conflict1781K → E in AAH22877. Ref.6
Sequence conflict3771I → V in AAH22877. Ref.6
Sequence conflict6651H → L in BAC11269. Ref.3
Sequence conflict696 – 6972SI → NS in AAD41245. Ref.1
Sequence conflict7391S → G in BAA91135. Ref.2

Sequences

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

Last modified May 3, 2011. Version 3.
Checksum: 6E1D26C87FF5D9C5

FASTA74784,881
        10         20         30         40         50         60 
MWGFLKRPVV VTADINLSLV ALTGMGLLSR LWRLTYPRAV VFDEVYYGQY ISFYMKQIFF 

        70         80         90        100        110        120 
LDDSGPPFGH MVLALGGYLG GFDGNFLWNR IGAEYSSNVP VWSLRLLPAL AGALSVPMAY 

       130        140        150        160        170        180 
QIVLELHFSH CAAMGAALLM LIENALITQS RLMLLESVLI FFNLLAVLSY LKFFNCQKHS 

       190        200        210        220        230        240 
PFSLSWWFWL TLTGVACSCA VGIKYMGVFT YVLVLGVAAV HAWHLLGDQT LSNVGADVQC 

       250        260        270        280        290        300 
CMRPACMGQM QMSQGVCVFC HLLARAVALL VIPVVLYLLF FYVHLILVFR SGPHDQIMSS 

       310        320        330        340        350        360 
AFQASLEGGL ARITQGQPLE VAFGSQVTLR NVFGKPVPCW LHSHQDTYPM IYENGRGSSH 

       370        380        390        400        410        420 
QQQVTCYPFK DVNNWWIVKD PRRHQLVVSS PPRPVRHGDM VQLVHGMTTR SLNTHDVAAP 

       430        440        450        460        470        480 
LSPHSQEVSC YIDYNISMPA QNLWRLEIVN RGSDTDVWKT ILSEVRFVHV NTSAVLKLSG 

       490        500        510        520        530        540 
AHLPDWGYRQ LEIVGEKLSR GYHGSTVWNV EEHRYGASQE QRERERELHS PAQVDVSRNL 

       550        560        570        580        590        600 
SFMARFSELQ WRMLALRSDD SEHKYSSSPL EWVTLDTNIA YWLHPRTSAQ IHLLGNIVIW 

       610        620        630        640        650        660 
VSGSLALAIY ALLSLWYLLR RRRNVHDLPQ DAWLRWVLAG ALCAGGWAVN YLPFFLMEKT 

       670        680        690        700        710        720 
LFLYHYLPAL TFQILLLPVV LQHISDHLCR SQLQRSIFSA LVVAWYSSAC HVSNTLRPLT 

       730        740 
YGDKSLSPHE LKALRWKDSW DILIRKH 

« Hide

Isoform 2 [UniParc].

Checksum: B58F992ADA9DF552
Show »

FASTA72582,567
Isoform 3 [UniParc].

Checksum: 51114C186E12533A
Show »

FASTA67176,294
Isoform 4 [UniParc].

Checksum: 1A8B7C19BF49EBC2
Show »

FASTA60869,531

References

« Hide 'large scale' references
[1]"Identification of a human homolog of the Drosophila rotated abdomen gene (POMT1) encoding a putative protein O-mannosyl-transferase, and assignment to human chromosome 9q34.1."
Perez Jurado L.A., Coloma A., Cruces J.
Genomics 58:171-180(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, VARIANT ARG-251.
Tissue: Fetal brain.
[2]"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 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 53-747 (ISOFORM 1), VARIANT ARG-251.
Tissue: Hippocampus, Ileal mucosa, Signet-ring cell carcinoma and Teratocarcinoma.
[3]"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
[4]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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 2).
Tissue: Testis and Uterus.
[7]"Mutations in the O-mannosyltransferase gene POMT1 give rise to the severe neuronal migration disorder Walker-Warburg syndrome."
Beltran-Valero de Bernabe D., Currier S., Steinbrecher A., Celli J., van Beusekom E., van der Zwaag B., Kayserili H., Merlini L., Chitayat D., Dobyns W.B., Cormand B., Lehesjoki A.-E., Cruces J., Voit T., Walsh C.A., van Bokhoven H., Brunner H.G.
Am. J. Hum. Genet. 71:1033-1043(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, VARIANTS MDDGA1 ARG-76 AND ASP-428.
[8]"Demonstration of mammalian protein O-mannosyltransferase activity: coexpression of POMT1 and POMT2 required for enzymatic activity."
Manya H., Chiba A., Yoshida A., Wang X., Chiba Y., Jigami Y., Margolis R.U., Endo T.
Proc. Natl. Acad. Sci. U.S.A. 101:500-505(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBCELLULAR LOCATION.
[9]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-471.
Tissue: Liver.
[10]"POMT1 mutation results in defective glycosylation and loss of laminin-binding activity in alpha-DG."
Kim D.-S., Hayashi Y.K., Matsumoto H., Ogawa M., Noguchi S., Murakami N., Sakuta R., Mochizuki M., Michele D.E., Campbell K.P., Nonaka I., Nishino I.
Neurology 62:1009-1011(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MDDGA1 LEU-421 DEL.
[11]"Mutations in POMT1 are found in a minority of patients with Walker-Warburg syndrome."
Currier S.C., Lee C.K., Chang B.S., Bodell A.L., Pai G.S., Job L., Lagae L.G., Al-Gazali L.I., Eyaid W.M., Enns G., Dobyns W.B., Walsh C.A.
Am. J. Med. Genet. A 133:53-57(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MDDGA1 ARG-537.
[12]"An autosomal recessive limb girdle muscular dystrophy (LGMD2) with mild mental retardation is allelic to Walker-Warburg syndrome (WWS) caused by a mutation in the POMT1 gene."
Balci B., Uyanik G., Dincer P., Gross C., Willer T., Talim B., Haliloglu G., Kale G., Hehr U., Winkler J., Topaloglu H.
Neuromuscul. Disord. 15:271-275(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MDDGC1 PRO-200.
[13]"The expanding phenotype of POMT1 mutations: from Walker-Warburg syndrome to congenital muscular dystrophy, microcephaly, and mental retardation."
van Reeuwijk J., Maugenre S., van den Elzen C., Verrips A., Bertini E., Muntoni F., Merlini L., Scheffer H., Brunner H.G., Guicheney P., van Bokhoven H.
Hum. Mutat. 27:453-459(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MDDGB1 ARG-65; MET-140 DEL; CYS-582 AND HIS-590, VARIANTS MDDGA1 CYS-105; HIS-105 AND VAL-207, VARIANTS PHE-285 AND LYS-522.
[14]"Expanding the clinical spectrum of POMT1 phenotype."
D'Amico A., Tessa A., Bruno C., Petrini S., Biancheri R., Pane M., Pedemonte M., Ricci E., Falace A., Rossi A., Mercuri E., Santorelli F.M., Bertini E.
Neurology 66:1564-1567(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MDDGB1 ARG-65; HIS-590 AND THR-669.
[15]"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: VARIANTS MDDGB1 ARG-65 AND ARG-537.
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF095136 mRNA. Translation: AAD41245.1.
AF095150 expand/collapse EMBL AC list , AF095138, AF095139, AF095140, AF095141, AF095142, AF095143, AF095144, AF095145, AF095146, AF095147, AF095148, AF095149 Genomic DNA. Translation: AAD41246.1.
AK000391 mRNA. Translation: BAA91135.1. Different initiation.
AK000475 mRNA. Translation: BAA91190.1. Different initiation.
AK295561 mRNA. Translation: BAG58462.1.
AK074874 mRNA. Translation: BAG52022.1.
AK074888 mRNA. Translation: BAC11269.1.
AL358781 Genomic DNA. Translation: CAI40220.1.
AL358781 Genomic DNA. Translation: CAI40221.1.
AL358781 Genomic DNA. Translation: CAI40223.1.
CH471090 Genomic DNA. Translation: EAW87978.1.
BC022877 mRNA. Translation: AAH22877.3.
BC065268 mRNA. Translation: AAH65268.1.
CCDSCCDS43894.1. [Q9Y6A1-2]
CCDS43895.1. [Q9Y6A1-3]
CCDS48045.1. [Q9Y6A1-4]
CCDS6943.1. [Q9Y6A1-1]
RefSeqNP_001070833.1. NM_001077365.1. [Q9Y6A1-2]
NP_001070834.1. NM_001077366.1. [Q9Y6A1-3]
NP_001129585.1. NM_001136113.1. [Q9Y6A1-2]
NP_001129586.1. NM_001136114.1. [Q9Y6A1-4]
NP_009102.3. NM_007171.3.
XP_005272213.1. XM_005272156.1. [Q9Y6A1-1]
UniGeneHs.522449.

3D structure databases

ProteinModelPortalQ9Y6A1.
SMRQ9Y6A1. Positions 319-476.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115834. 2 interactions.
IntActQ9Y6A1. 1 interaction.

Protein family/group databases

CAZyGT39. Glycosyltransferase Family 39.

PTM databases

PhosphoSiteQ9Y6A1.

Polymorphism databases

DMDM332278226.

Proteomic databases

MaxQBQ9Y6A1.
PaxDbQ9Y6A1.
PRIDEQ9Y6A1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000341012; ENSP00000343034; ENSG00000130714. [Q9Y6A1-3]
ENST00000372228; ENSP00000361302; ENSG00000130714. [Q9Y6A1-1]
ENST00000402686; ENSP00000385797; ENSG00000130714. [Q9Y6A1-2]
ENST00000404875; ENSP00000384531; ENSG00000130714. [Q9Y6A1-4]
ENST00000423007; ENSP00000404119; ENSG00000130714. [Q9Y6A1-2]
GeneID10585.
KEGGhsa:10585.
UCSCuc004cau.3. human. [Q9Y6A1-2]
uc004cav.3. human. [Q9Y6A1-1]
uc004caw.3. human. [Q9Y6A1-3]
uc011mck.2. human. [Q9Y6A1-4]

Organism-specific databases

CTD10585.
GeneCardsGC09P134378.
GeneReviewsPOMT1.
HGNCHGNC:9202. POMT1.
MIM236670. phenotype.
607423. gene.
609308. phenotype.
613155. phenotype.
neXtProtNX_Q9Y6A1.
Orphanet86812. Autosomal recessive limb-girdle muscular dystrophy type 2K.
370959. Congenital muscular dystrophy with cerebellar involvement.
370968. Congenital muscular dystrophy with intellectual disability.
370980. Congenital muscular dystrophy without intellectual disability.
588. Muscle-eye-brain disease.
899. Walker-Warburg syndrome.
PharmGKBPA33527.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1928.
HOVERGENHBG053637.
InParanoidQ9Y6A1.
KOK00728.
OMALLFFYVH.
OrthoDBEOG79KPDP.
PhylomeDBQ9Y6A1.
TreeFamTF300552.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ9Y6A1.
BgeeQ9Y6A1.
GenevestigatorQ9Y6A1.

Family and domain databases

InterProIPR027005. GlyclTrfase_39_like.
IPR003342. Glyco_trans_39.
IPR016093. MIR_motif.
[Graphical view]
PANTHERPTHR10050. PTHR10050. 1 hit.
PfamPF02815. MIR. 1 hit.
PF02366. PMT. 1 hit.
[Graphical view]
SMARTSM00472. MIR. 3 hits.
[Graphical view]
SUPFAMSSF82109. SSF82109. 1 hit.
PROSITEPS50919. MIR. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPOMT1. human.
GeneWikiPOMT1.
GenomeRNAi10585.
NextBio40189.
PROQ9Y6A1.
SOURCESearch...

Entry information

Entry namePOMT1_HUMAN
AccessionPrimary (citable) accession number: Q9Y6A1
Secondary accession number(s): B3KQG0 expand/collapse secondary AC list , B4DIF0, Q5JT01, Q5JT06, Q5JT08, Q8NC91, Q8TCA9, Q9NX32, Q9NX82, Q9UNT2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: May 3, 2011
Last modified: July 9, 2014
This is version 134 of the entry and version 3 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 9

Human chromosome 9: entries, gene names and cross-references to MIM