Q9Y6A1 (POMT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein O-mannosyl-transferase 1
EC=2.4.1.109

Alternative name(s):
Dolichyl-phosphate-mannose--protein mannosyltransferase 1

Gene names

Name:

POMT1

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	747 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Cofactor	Magnesium. Manganese and calcium ions suppress enzyme activity.
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 component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Congenital muscular dystrophy Disease mutation Limb-girdle muscular dystrophy Lissencephaly
Domain	Repeat Transmembrane Transmembrane helix
Ligand	Magnesium Metal-binding
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	extracellular matrix organization Inferred from electronic annotation. Source: Compara multicellular organismal development Traceable author statement Ref.1. Source: ProtInc protein O-linked glycosylation Traceable author statement Ref.1. Source: ProtInc
Cellular_component	acrosomal vesicle Inferred from electronic annotation. Source: Compara endoplasmic reticulum membrane Inferred from direct assay Ref.8. Source: UniProtKB integral to membrane Traceable author statement Ref.1. Source: ProtInc sarcoplasmic reticulum Inferred from electronic annotation. Source: Compara
Molecular_function	dolichyl-phosphate-mannose-protein mannosyltransferase activity Inferred from electronic annotation. Source: 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 747	747	Protein O-mannosyl-transferase 1		PRO_0000121484
Regions
	Transmembrane	8 – 28	21	Helical; Potential
	Transmembrane	40 – 60	21	Helical; Potential
	Transmembrane	68 – 88	21	Helical; Potential
	Transmembrane	99 – 119	21	Helical; Potential
	Transmembrane	122 – 142	21	Helical; Potential
	Transmembrane	154 – 174	21	Helical; Potential
	Transmembrane	183 – 203	21	Helical; Potential
	Transmembrane	206 – 226	21	Helical; Potential
	Transmembrane	269 – 289	21	Helical; Potential
	Transmembrane	597 – 617	21	Helical; Potential
	Transmembrane	636 – 656	21	Helical; Potential
	Transmembrane	661 – 681	21	Helical; Potential
	Domain	318 – 381	64	MIR 1
	Domain	392 – 449	58	MIR 2
	Domain	453 – 513	61	MIR 3
Amino acid modifications
	Glycosylation	435	1	N-linked (GlcNAc...) Potential
	Glycosylation	471	1	N-linked (GlcNAc...) Ref.9
	Glycosylation	539	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	1 – 117	117	Missing in isoform 4.		VSP_041024
	Alternative sequence	1 – 54	54	Missing in isoform 3.		VSP_007590
	Alternative sequence	234 – 255	22	Missing in isoform 2, isoform 3 and isoform 4.		VSP_007591
	Natural variant	65	1	G → R in MDDGB1. Ref.13 Ref.14 Ref.15		VAR_065027
	Natural variant	76	1	G → R in MDDGA1. Ref.7 Corresponds to variant rs28941782 [ dbSNP | Ensembl ].		VAR_015734
	Natural variant	105	1	R → C in MDDGA1; severe Walker-Warburg syndrome. Ref.13		VAR_065028
	Natural variant	105	1	R → H in MDDGA1; severe Walker-Warburg syndrome. Ref.13		VAR_065029
	Natural variant	140	1	Missing in MDDGB1. Ref.13		VAR_065030
	Natural variant	200	1	A → P in MDDGC1; a common founder mutation. Ref.12		VAR_022661
	Natural variant	207	1	G → V in MDDGA1; severe Walker-Warburg syndrome. Ref.13		VAR_065031
	Natural variant	251	1	Q → R. Ref.1 Ref.2 Corresponds to variant rs2296949 [ dbSNP | Ensembl ].		VAR_034390
	Natural variant	251	1	Q → W Requires 2 nucleotide substitutions. Corresponds to variant rs3887873 [ dbSNP | Ensembl ].		VAR_034389
	Natural variant	285	1	L → F. Ref.13		VAR_065032
	Natural variant	327	1	V → I. Corresponds to variant rs4740164 [ dbSNP | Ensembl ].		VAR_034391
	Natural variant	421	1	Missing in MDDGA1; associated with the loss of function of alpha dystroglycan as a matrix receptor. Ref.10		VAR_022662
	Natural variant	428	1	V → D in MDDGA1. Ref.7		VAR_015735
	Natural variant	433	1	D → E. Corresponds to variant rs11243406 [ dbSNP | Ensembl ].		VAR_034392
	Natural variant	522	1	R → K. Ref.13		VAR_065033
	Natural variant	537	1	S → R in MDDGA1 and MDDGB1. Ref.11 Ref.15		VAR_026697
	Natural variant	582	1	W → C in MDDGB1. Ref.13		VAR_065034
	Natural variant	590	1	Q → H in MDDGB1. Ref.13 Ref.14		VAR_065035
	Natural variant	669	1	A → T in MDDGB1. Ref.14		VAR_065036
Experimental info
	Sequence conflict	37	1	P → Q in AAH22877. Ref.6
	Sequence conflict	143	1	E → K in AAD41245. Ref.1
	Sequence conflict	147	1	I → V in BAG58462. Ref.2
	Sequence conflict	178	1	K → E in AAH22877. Ref.6
	Sequence conflict	377	1	I → V in AAH22877. Ref.6
	Sequence conflict	665	1	H → L in BAC11269. Ref.3
	Sequence conflict	696 – 697	2	SI → NS in AAD41245. Ref.1
	Sequence conflict	739	1	S → G in BAA91135. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 3, 2011. Version 3. Checksum: 6E1D26C87FF5D9C5	FASTA	747	84,881
	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
	Isoform 2 [UniParc]. Checksum: B58F992ADA9DF552	FASTA	725	82,567
	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 LSNVCVFCHL 250 260 270 280 290 300 LARAVALLVI PVVLYLLFFY VHLILVFRSG PHDQIMSSAF QASLEGGLAR ITQGQPLEVA 310 320 330 340 350 360 FGSQVTLRNV FGKPVPCWLH SHQDTYPMIY ENGRGSSHQQ QVTCYPFKDV NNWWIVKDPR 370 380 390 400 410 420 RHQLVVSSPP RPVRHGDMVQ LVHGMTTRSL NTHDVAAPLS PHSQEVSCYI DYNISMPAQN 430 440 450 460 470 480 LWRLEIVNRG SDTDVWKTIL SEVRFVHVNT SAVLKLSGAH LPDWGYRQLE IVGEKLSRGY 490 500 510 520 530 540 HGSTVWNVEE HRYGASQEQR ERERELHSPA QVDVSRNLSF MARFSELQWR MLALRSDDSE 550 560 570 580 590 600 HKYSSSPLEW VTLDTNIAYW LHPRTSAQIH LLGNIVIWVS GSLALAIYAL LSLWYLLRRR 610 620 630 640 650 660 RNVHDLPQDA WLRWVLAGAL CAGGWAVNYL PFFLMEKTLF LYHYLPALTF QILLLPVVLQ 670 680 690 700 710 720 HISDHLCRSQ LQRSIFSALV VAWYSSACHV SNTLRPLTYG DKSLSPHELK ALRWKDSWDI LIRKH
	Isoform 3 [UniParc]. Checksum: 51114C186E12533A	FASTA	671	76,294
	10 20 30 40 50 60 MKQIFFLDDS GPPFGHMVLA LGGYLGGFDG NFLWNRIGAE YSSNVPVWSL RLLPALAGAL 70 80 90 100 110 120 SVPMAYQIVL ELHFSHCAAM GAALLMLIEN ALITQSRLML LESVLIFFNL LAVLSYLKFF 130 140 150 160 170 180 NCQKHSPFSL SWWFWLTLTG VACSCAVGIK YMGVFTYVLV LGVAAVHAWH LLGDQTLSNV 190 200 210 220 230 240 CVFCHLLARA VALLVIPVVL YLLFFYVHLI LVFRSGPHDQ IMSSAFQASL EGGLARITQG 250 260 270 280 290 300 QPLEVAFGSQ VTLRNVFGKP VPCWLHSHQD TYPMIYENGR GSSHQQQVTC YPFKDVNNWW 310 320 330 340 350 360 IVKDPRRHQL VVSSPPRPVR HGDMVQLVHG MTTRSLNTHD VAAPLSPHSQ EVSCYIDYNI 370 380 390 400 410 420 SMPAQNLWRL EIVNRGSDTD VWKTILSEVR FVHVNTSAVL KLSGAHLPDW GYRQLEIVGE 430 440 450 460 470 480 KLSRGYHGST VWNVEEHRYG ASQEQRERER ELHSPAQVDV SRNLSFMARF SELQWRMLAL 490 500 510 520 530 540 RSDDSEHKYS SSPLEWVTLD TNIAYWLHPR TSAQIHLLGN IVIWVSGSLA LAIYALLSLW 550 560 570 580 590 600 YLLRRRRNVH DLPQDAWLRW VLAGALCAGG WAVNYLPFFL MEKTLFLYHY LPALTFQILL 610 620 630 640 650 660 LPVVLQHISD HLCRSQLQRS IFSALVVAWY SSACHVSNTL RPLTYGDKSL SPHELKALRW 670 KDSWDILIRK H
	Isoform 4 [UniParc]. Checksum: 1A8B7C19BF49EBC2	FASTA	608	69,531
	10 20 30 40 50 60 MAYQIVLELH FSHCAAMGAA LLMLIENALI TQSRLMLLES VLIFFNLLAV LSYLKFFNCQ 70 80 90 100 110 120 KHSPFSLSWW FWLTLTGVAC SCAVGIKYMG VFTYVLVLGV AAVHAWHLLG DQTLSNVCVF 130 140 150 160 170 180 CHLLARAVAL LVIPVVLYLL FFYVHLILVF RSGPHDQIMS SAFQASLEGG LARITQGQPL 190 200 210 220 230 240 EVAFGSQVTL RNVFGKPVPC WLHSHQDTYP MIYENGRGSS HQQQVTCYPF KDVNNWWIVK 250 260 270 280 290 300 DPRRHQLVVS SPPRPVRHGD MVQLVHGMTT RSLNTHDVAA PLSPHSQEVS CYIDYNISMP 310 320 330 340 350 360 AQNLWRLEIV NRGSDTDVWK TILSEVRFVH VNTSAVLKLS GAHLPDWGYR QLEIVGEKLS 370 380 390 400 410 420 RGYHGSTVWN VEEHRYGASQ EQRERERELH SPAQVDVSRN LSFMARFSEL QWRMLALRSD 430 440 450 460 470 480 DSEHKYSSSP LEWVTLDTNI AYWLHPRTSA QIHLLGNIVI WVSGSLALAI YALLSLWYLL 490 500 510 520 530 540 RRRRNVHDLP QDAWLRWVLA GALCAGGWAV NYLPFFLMEK TLFLYHYLPA LTFQILLLPV 550 560 570 580 590 600 VLQHISDHLC RSQLQRSIFS ALVVAWYSSA CHVSNTLRPL TYGDKSLSPH ELKALRWKDS WDILIRKH

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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, 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, MASS SPECTROMETRY. 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. , 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

GeneReviews

GGDB

GlycoGene database

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF095136 mRNA. Translation: AAD41245.1. AF095150 , 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.
IPI	IPI00298235. IPI00329484. IPI00329485. IPI00642847.
RefSeq	NP_001070833.1. NM_001077365.1. NP_001070834.1. NM_001077366.1. NP_001129585.1. NM_001136113.1. NP_001129586.1. NM_001136114.1. NP_009102.3. NM_007171.3.
UniGene	Hs.522449.
3D structure databases
ProteinModelPortal	Q9Y6A1.
SMR	Q9Y6A1. Positions 319-476.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y6A1. 1 interaction.
Protein family/group databases
CAZy	GT39. Glycosyltransferase Family 39.
PTM databases
PhosphoSite	Q9Y6A1.
Polymorphism databases
DMDM	32171725.
Proteomic databases
PaxDb	Q9Y6A1.
PRIDE	Q9Y6A1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000341012; ENSP00000343034; ENSG00000130714. ENST00000372228; ENSP00000361302; ENSG00000130714. ENST00000402686; ENSP00000385797; ENSG00000130714. ENST00000404875; ENSP00000384531; ENSG00000130714. ENST00000423007; ENSP00000404119; ENSG00000130714.
GeneID	10585.
KEGG	hsa:10585.
UCSC	uc004cau.3. human. uc004cav.3. human. uc004caw.3. human. uc011mck.2. human.
Organism-specific databases
CTD	10585.
GeneCards	GC09P134378.
HGNC	HGNC:9202. POMT1.
MIM	236670. phenotype. 607423. gene. 609308. phenotype. 613155. phenotype.
neXtProt	NX_Q9Y6A1.
Orphanet	86812. Autosomal recessive limb-girdle muscular dystrophy type 2K. 899. Walker-Warburg syndrome.
PharmGKB	PA33527.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1928.
HOVERGEN	HBG053637.
InParanoid	Q9Y6A1.
KO	K00728.
OMA	PMAYQIV.
PhylomeDB	Q9Y6A1.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	Q9Y6A1.
Bgee	Q9Y6A1.
Genevestigator	Q9Y6A1.
GermOnline	ENSG00000130714. Homo sapiens.
Family and domain databases
InterPro	IPR027005. GlyclTrfase_39_like. IPR003342. Glyco_trans_39. IPR016093. MIR_motif. [Graphical view]
PANTHER	PTHR10050. PTHR10050. 1 hit.
Pfam	PF02815. MIR. 1 hit. PF02366. PMT. 1 hit. [Graphical view]
SMART	SM00472. MIR. 3 hits. [Graphical view]
SUPFAM	SSF82109. MIR. 1 hit.
PROSITE	PS50919. MIR. 3 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	POMT1. human.
GenomeRNAi	10585.
NextBio	40189.
SOURCE	Search...

Entry information

Entry name

POMT1_HUMAN

Accession

Primary (citable) accession number: Q9Y6A1
Secondary accession number(s): B3KQG0 , 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:	May 1, 2013
This is version 120 of the entry and version 3 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.