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Q9UKY4 (POMT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. 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 2

EC=2.4.1.109
Alternative name(s):
Dolichyl-phosphate-mannose--protein mannosyltransferase 2
Gene names
Name:POMT2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length750 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.6

Catalytic activity

Dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein. Ref.6

Enzyme regulation

Slightly activated by Mg2+ and inhibited by both Ca+ and Mn2+. EDTA ha no effect on activity in vitro. Ref.6

Pathway

Protein modification; protein glycosylation.

Subunit structure

Interacts with POMT1 Probable.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.1 Ref.6.

Tissue specificity

Highly expressed in testis; detected at low levels in most tissues.

Post-translational modification

N-glycosylated. Ref.1

Involvement in disease

Muscular dystrophy-dystroglycanopathy congenital with brain and eye anomalies A2 (MDDGA2) [MIM:613150]: 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. Ref.7 Ref.8 Ref.10 Ref.12 Ref.14

Muscular dystrophy-dystroglycanopathy congenital with mental retardation B2 (MDDGB2) [MIM:613156]: 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.

Muscular dystrophy-dystroglycanopathy limb-girdle C2 (MDDGC2) [MIM:613158]: An autosomal recessive muscular dystrophy with onset after ambulation is achieved. MDDGC2 is characterized by increased serum creatine kinase and mild muscle weakness. Muscle biopsy shows dystrophic changes, inflammatory changes, and severely decreased alpha-dystroglycan. Cognition is normal.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.10

Sequence similarities

Belongs to the glycosyltransferase 39 family.

Contains 3 MIR domains.

Sequence caution

The sequence CAD62348.1 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UKY4-1)

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: Q9UKY4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     83-750: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 750750Protein O-mannosyl-transferase 2
PRO_0000121488

Regions

Transmembrane54 – 7421Helical; Potential
Transmembrane100 – 12021Helical; Potential
Transmembrane146 – 16621Helical; Potential
Transmembrane191 – 21121Helical; Potential
Transmembrane231 – 25121Helical; Potential
Transmembrane283 – 30321Helical; Potential
Transmembrane596 – 61621Helical; Potential
Transmembrane643 – 66321Helical; Potential
Transmembrane665 – 68521Helical; Potential
Transmembrane700 – 72021Helical; Potential
Domain334 – 39057MIR 1
Domain403 – 45957MIR 2
Domain464 – 52158MIR 3

Amino acid modifications

Glycosylation981N-linked (GlcNAc...) Potential
Glycosylation3301N-linked (GlcNAc...) Potential
Glycosylation4451N-linked (GlcNAc...) Potential
Glycosylation5281N-linked (GlcNAc...) Potential
Glycosylation5831N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence83 – 750668Missing in isoform 2.
VSP_041457
Natural variant541A → E.
Corresponds to variant rs8177536 [ dbSNP | Ensembl ].
VAR_022083
Natural variant1841T → M in MDDGC2. Ref.9 Ref.10
VAR_065037
Natural variant1981I → N in MDDGA2. Ref.10
VAR_065038
Natural variant2461G → D in MDDGB2. Ref.13
VAR_065039
Natural variant3531G → S in MDDGA2. Ref.8 Ref.13
VAR_065040
Natural variant3731V → F in MDDGA2. Ref.10
VAR_065041
Natural variant4131R → P in MDDGA2. Ref.10
Corresponds to variant rs190285831 [ dbSNP | Ensembl ].
VAR_065042
Natural variant444 – 4452IN → LLWQ in MDDGA2.
VAR_065043
Natural variant4781H → R in MDDGA2. Ref.14
VAR_068968
Natural variant4821G → V in MDDGA2. Ref.12
VAR_065044
Natural variant6661Y → C in MDDGB2 and MDDGA2. Ref.10 Ref.11 Ref.12 Ref.13
VAR_065045
Natural variant7171F → S in MDDGB2.
VAR_065046
Natural variant7261G → E in MDDGA2 and MDDGB2. Ref.8 Ref.13
VAR_065047
Natural variant7481W → R in MDDGB2. Ref.11
VAR_065048
Natural variant7481W → S in MDDGC2. Ref.10
VAR_065049

Experimental info

Sequence conflict531E → Q in AAF14118. Ref.1
Sequence conflict531E → Q in AAM12046. Ref.1

Sequences

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

Last modified June 20, 2003. Version 2.
Checksum: 79732D6C4978CFB9

FASTA75084,214
        10         20         30         40         50         60 
MPPATGGGLA ESELRPRRGR CGPQAARAAG RDVAAEAVAR SPKRPAWGSR RFEAVGWWAL 

        70         80         90        100        110        120 
LALVTLLSFA TRFHRLDEPP HICWDETHFG KMGSYYINRT FFFDVHPPLG KMLIGLAGYL 

       130        140        150        160        170        180 
SGYDGTFLFQ KPGDKYEHHS YMGMRGFCAF LGSWLVPFAY LTVLDLSKSL SAALLTAALL 

       190        200        210        220        230        240 
TFDTGCLTLS QYILLDPILM FFIMAAMLSM VKYNSCADRP FSAPWWFWLS LTGVSLAGAL 

       250        260        270        280        290        300 
GVKFVGLFII LQVGLNTIAD LWYLFGDLSL SLVTVGKHLT ARVLCLIVLP LALYTATFAV 

       310        320        330        340        350        360 
HFMVLSKSGP GDGFFSSAFQ ARLSGNNLHN ASIPEHLAYG SVITVKNLRM AIGYLHSHRH 

       370        380        390        400        410        420 
LYPEGIGARQ QQVTTYLHKD YNNLWIIKKH NTNSDPLDPS FPVEFVRHGD IIRLEHKETS 

       430        440        450        460        470        480 
RNLHSHYHEA PMTRKHYQVT GYGINGTGDS NDFWRIEVVN RKFGNRIKVL RSRIRFIHLV 

       490        500        510        520        530        540 
TGCVLGSSGK VLPKWGWEQL EVTCTPYLKE TLNSIWNVED HINPKLPNIS LDVLQPSFPE 

       550        560        570        580        590        600 
ILLESHMVMI RGNSGLKPKD NEFTSKPWHW PINYQGLRFS GVNDTDFRVY LLGNPVVWWL 

       610        620        630        640        650        660 
NLLSIALYLL SGSIIAVAMQ RGARLPAEVA GLSQVLLRGG GQVLLGWTLH YFPFFLMGRV 

       670        680        690        700        710        720 
LYFHHYFPAM LFSSMLTGIL WDTLLRLCAW GLASWPLARG IHVAGILSLL LGTAYSFYLF 

       730        740        750 
HPLAYGMVGP LAQDPQSPMA GLRWLDSWDF 

« Hide

Isoform 2 [UniParc].

Checksum: FFC305699BA89C4F
Show »

FASTA828,899

References

« Hide 'large scale' references
[1]"Characterization of POMT2, a novel member of the PMT protein O-mannosyltransferase family specifically localized to the acrosome of mammalian spermatids."
Willer T., Amselgruber W., Deutzmann R., Strahl S.
Glycobiology 12:771-783(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), GLYCOSYLATION, SUBCELLULAR LOCATION.
Tissue: Cerebellum.
[2]"Full-length cDNA libraries and normalization."
Li W.B., Gruber C., Jessee J., Polayes D.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Neuroblastoma.
[3]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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).
Tissue: Brain.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 612-750.
Tissue: Testis.
[6]"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.
[7]"POMT2 mutations cause alpha-dystroglycan hypoglycosylation and Walker-Warburg syndrome."
van Reeuwijk J., Janssen M., van den Elzen C., Beltran-Valero de Bernabe D., Sabatelli P., Merlini L., Boon M., Scheffer H., Brockington M., Muntoni F., Huynen M.A., Verrips A., Walsh C.A., Barth P.G., Brunner H.G., van Bokhoven H.
J. Med. Genet. 42:907-912(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MDDGA2.
[8]"POMT2 mutation in a patient with 'MEB-like' phenotype."
Mercuri E., D'Amico A., Tessa A., Berardinelli A., Pane M., Messina S., van Reeuwijk J., Bertini E., Muntoni F., Santorelli F.M.
Neuromuscul. Disord. 16:446-448(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MDDGA2 SER-353 AND GLU-726.
[9]"POMT2 gene mutation in limb-girdle muscular dystrophy with inflammatory changes."
Biancheri R., Falace A., Tessa A., Pedemonte M., Scapolan S., Cassandrini D., Aiello C., Rossi A., Broda P., Zara F., Santorelli F.M., Minetti C., Bruno C.
Biochem. Biophys. Res. Commun. 363:1033-1037(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MDDGC2 MET-184.
[10]"Refining genotype phenotype correlations in muscular dystrophies with defective glycosylation of dystroglycan."
Godfrey C., Clement E., Mein R., Brockington M., Smith J., Talim B., Straub V., Robb S., Quinlivan R., Feng L., Jimenez-Mallebrera C., Mercuri E., Manzur A.Y., Kinali M., Torelli S., Brown S.C., Sewry C.A., Bushby K. expand/collapse author list , Topaloglu H., North K., Abbs S., Muntoni F.
Brain 130:2725-2735(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MDDGA2 ASN-198; PHE-373; PRO-413 AND CYS-666, VARIANTS MDDGC2 MET-184 AND SER-748.
[11]"New POMT2 mutations causing congenital muscular dystrophy: identification of a founder mutation."
Yanagisawa A., Bouchet C., Van den Bergh P.Y., Cuisset J.M., Viollet L., Leturcq F., Romero N.B., Quijano-Roy S., Fardeau M., Seta N., Guicheney P.
Neurology 69:1254-1260(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MDDGB2 CYS-666 AND ARG-748.
[12]"POMT2 intragenic deletions and splicing abnormalities causing congenital muscular dystrophy with mental retardation."
Yanagisawa A., Bouchet C., Quijano-Roy S., Vuillaumier-Barrot S., Clarke N., Odent S., Rodriguez D., Romero N.B., Osawa M., Endo T., Taratuto A.L., Seta N., Guicheney P.
Eur. J. Med. Genet. 52:201-206(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MDDGA2 VAL-482; 444-ILE-ASN-445 DELINS LEU-LEU-TRP-GLN AND CYS-666.
[13]"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 MDDGB2 ASP-246; SER-353; CYS-666 AND GLU-726.
[14]"Exome sequencing and functional validation in zebrafish identify GTDC2 mutations as a cause of Walker-Warburg syndrome."
Manzini M.C., Tambunan D.E., Hill R.S., Yu T.W., Maynard T.M., Heinzen E.L., Shianna K.V., Stevens C.R., Partlow J.N., Barry B.J., Rodriguez J., Gupta V.A., Al-Qudah A.K., Eyaid W.M., Friedman J.M., Salih M.A., Clark R., Moroni I. expand/collapse author list , Mora M., Beggs A.H., Gabriel S.B., Walsh C.A.
Am. J. Hum. Genet. 91:541-547(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MDDGA2 ARG-478.
+Additional computationally mapped references.

Web resources

GeneReviews
GGDB

GlycoGene database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF105020 mRNA. Translation: AAF14118.1.
AY090480 mRNA. Translation: AAM12046.1.
BX248027 mRNA. Translation: CAD62348.1. Sequence problems.
AC007954 Genomic DNA. Translation: AAF62558.1.
AC007375 Genomic DNA. Translation: AAF63184.1.
BC031651 mRNA. Translation: AAH31651.1.
AL353956 mRNA. Translation: CAB89256.1.
PIRT48691.
RefSeqNP_037514.2. NM_013382.5.
UniGeneHs.132989.

3D structure databases

ProteinModelPortalQ9UKY4.
SMRQ9UKY4. Positions 334-522.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118991. 1 interaction.
STRING9606.ENSP00000261534.

Protein family/group databases

CAZyGT39. Glycosyltransferase Family 39.

PTM databases

PhosphoSiteQ9UKY4.

Polymorphism databases

DMDM32171723.

Proteomic databases

PaxDbQ9UKY4.
PRIDEQ9UKY4.

Protocols and materials databases

DNASU29954.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261534; ENSP00000261534; ENSG00000009830. [Q9UKY4-1]
ENST00000556326; ENSP00000450630; ENSG00000009830. [Q9UKY4-2]
GeneID29954.
KEGGhsa:29954.
UCSCuc001xth.1. human. [Q9UKY4-1]

Organism-specific databases

CTD29954.
GeneCardsGC14M077741.
H-InvDBHIX0011845.
HGNCHGNC:19743. POMT2.
HPAHPA003663.
MIM607439. gene.
613150. phenotype.
613156. phenotype.
613158. phenotype.
neXtProtNX_Q9UKY4.
Orphanet206559. Autosomal recessive limb-girdle muscular dystrophy type 2N.
370959. Congenital muscular dystrophy with cerebellar involvement.
370968. Congenital muscular dystrophy with intellectual disability.
588. Muscle-eye-brain disease.
899. Walker-Warburg syndrome.
PharmGKBPA134980627.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1928.
HOGENOMHOG000157526.
HOVERGENHBG096391.
InParanoidQ9UKY4.
KOK00728.
OMAWLCISRF.
OrthoDBEOG79KPDP.
PhylomeDBQ9UKY4.
TreeFamTF300552.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ9UKY4.
BgeeQ9UKY4.
CleanExHS_POMT2.
GenevestigatorQ9UKY4.

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

ChiTaRSPOMT2. human.
GeneWikiPOMT2.
GenomeRNAi29954.
NextBio52659.
PROQ9UKY4.
SOURCESearch...

Entry information

Entry namePOMT2_HUMAN
AccessionPrimary (citable) accession number: Q9UKY4
Secondary accession number(s): Q9NSG6, Q9P1W0, Q9P1W2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: June 20, 2003
Last modified: April 16, 2014
This is version 127 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 14

Human chromosome 14: entries, gene names and cross-references to MIM