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Q9NUD9 (PIGV_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GPI mannosyltransferase 2

EC=2.4.1.-
Alternative name(s):
GPI mannosyltransferase II
Short name=GPI-MT-II
Phosphatidylinositol-glycan biosynthesis class V protein
Short name=PIG-V
Gene names
Name:PIGV
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Alpha-1,6-mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly. Ref.6 Ref.7

Pathway

Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.7.

Post-translational modification

Not N-glycosylated. Ref.7

Involvement in disease

Hyperphosphatasia with mental retardation syndrome 1 (HPMRS1) [MIM:239300]: A severe syndrome characterized by elevated serum alkaline phosphatase, severe mental retardation, seizures, hypotonia, facial dysmorphism, and hypoplastic terminal phalanges.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9

Sequence similarities

Belongs to the PIGV family.

Sequence caution

The sequence CAI21625.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI21626.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI21627.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 493493GPI mannosyltransferase 2
PRO_0000246234

Regions

Topological domain1 – 1313Cytoplasmic Potential
Transmembrane14 – 3421Helical; Potential
Topological domain35 – 7743Lumenal Potential
Transmembrane78 – 9821Helical; Potential
Topological domain99 – 11315Cytoplasmic Potential
Transmembrane114 – 13421Helical; Potential
Topological domain135 – 1362Lumenal Potential
Transmembrane137 – 15721Helical; Potential
Topological domain158 – 1614Cytoplasmic Potential
Transmembrane162 – 18221Helical; Potential
Topological domain183 – 19210Lumenal Potential
Transmembrane193 – 21321Helical; Potential
Topological domain214 – 23421Cytoplasmic Potential
Transmembrane235 – 25521Helical; Potential
Topological domain256 – 32772Lumenal Potential
Transmembrane328 – 34821Helical; Potential
Topological domain349 – 37830Cytoplasmic Potential
Transmembrane379 – 39921Helical; Potential
Topological domain400 – 46970Lumenal Potential
Transmembrane470 – 49021Helical; Potential
Topological domain491 – 4933Cytoplasmic Potential

Natural variations

Natural variant2561Q → K in HPMRS1. Ref.9
VAR_064190
Natural variant3411A → E in HPMRS1. Ref.9
VAR_064191
Natural variant3411A → V in HPMRS1. Ref.9
VAR_064192
Natural variant3851H → P in HPMRS1. Ref.9
VAR_064193

Experimental info

Mutagenesis661W → L: Loss of function. Ref.7
Mutagenesis671D → A: Loss of function. Ref.7
Mutagenesis293 – 2942PP → TA: N-glycosylated due to the creation of an acceptor site for N-glycosylation.
Mutagenesis3081Q → A: Induces a reduces enzyme activity. Ref.7
Mutagenesis3121W → L: Loss of function. Ref.7
Sequence conflict331I → T in BAA91196. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9NUD9 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 087AE31E51BDD519

FASTA49355,713
        10         20         30         40         50         60 
MWPQDPSRKE VLRFAVSCRI LTLMLQALFN AIIPDHHAEA FSPPRLAPSG FVDQLVEGLL 

        70         80         90        100        110        120 
GGLSHWDAEH FLFIAEHGYL YEHNFAFFPG FPLALLVGTE LLRPLRGLLS LRSCLLISVA 

       130        140        150        160        170        180 
SLNFLFFMLA AVALHDLGCL VLHCPHQSFY AALLFCLSPA NVFLAAGYSE ALFALLTFSA 

       190        200        210        220        230        240 
MGQLERGRVW TSVLLFAFAT GVRSNGLVSV GFLMHSQCQG FFSSLTMLNP LRQLFKLMAS 

       250        260        270        280        290        300 
LFLSVFTLGL PFALFQYYAY TQFCLPGSAR PIPEPLVQLA VDKGYRIAEG NEPPWCFWDV 

       310        320        330        340        350        360 
PLIYSYIQDV YWNVGFLKYY ELKQVPNFLL AAPVAILVAW ATWTYVTTHP WLCLTLGLQR 

       370        380        390        400        410        420 
SKNNKTLEKP DLGFLSPQVF VYVVHAAVLL LFGGLCMHVQ VLTRFLGSST PIMYWFPAHL 

       430        440        450        460        470        480 
LQDQEPLLRS LKTVPWKPLA EDSPPGQKVP RNPIMGLLYH WKTCSPVTRY ILGYFLTYWL 

       490 
LGLLLHCNFL PWT 

« Hide

References

« Hide 'large scale' references
[1]"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].
[2]"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].
[3]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].
[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].
Tissue: Lung.
[5]"Familial hyperphosphatase with mental retardation, seizures, and neurologic deficits."
Mabry C.C., Bautista A., Kirk R.F., Dubilier L.D., Braunstein H., Koepke J.A.
J. Pediatr. 77:74-85(1970) [PubMed] [Europe PMC] [Abstract]
Cited for: DESCRIPTION OF HYPERPHOSPHATASIA WITH MENTAL RETARDATION SYNDROME.
[6]"Saccharomyces cerevisiae Ybr004c and its human homologue are required for addition of the second mannose during glycosylphosphatidylinositol precursor assembly."
Fabre A.-L., Orlean P., Taron C.H.
FEBS J. 272:1160-1168(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"PIG-V involved in transferring the second mannose in glycosylphosphatidylinositol."
Kang J.Y., Hong Y., Ashida H., Shishioh N., Murakami Y., Morita Y.S., Maeda Y., Kinoshita T.
J. Biol. Chem. 280:9489-9497(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, LACK OF GLYCOSYLATION, MUTAGENESIS OF TRP-66; ASP-67; 293-PRO-PRO-294; GLN-308 AND TRP-312.
[8]"Hyperphosphatasia with seizures, neurologic deficit, and characteristic facial features: Five new patients with Mabry syndrome."
Thompson M.D., Nezarati M.M., Gillessen-Kaesbach G., Meinecke P., Mendoza R., Mornet E., Brun-Heath I., Squarcioni C.P., Legeai-Mallet L., Munnich A., Cole D.E.
Am. J. Med. Genet. A 152:1661-1669(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: DESCRIPTION OF HYPERPHOSPHATASIA WITH MENTAL RETARDATION SYNDROME.
[9]"Identity-by-descent filtering of exome sequence data identifies PIGV mutations in hyperphosphatasia mental retardation syndrome."
Krawitz P.M., Schweiger M.R., Rodelsperger C., Marcelis C., Kolsch U., Meisel C., Stephani F., Kinoshita T., Murakami Y., Bauer S., Isau M., Fischer A., Dahl A., Kerick M., Hecht J., Kohler S., Jager M., Grunhagen J. expand/collapse author list , de Condor B.J., Doelken S., Brunner H.G., Meinecke P., Passarge E., Thompson M.D., Cole D.E., Horn D., Roscioli T., Mundlos S., Robinson P.N.
Nat. Genet. 42:827-829(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HPMRS1 LYS-256; VAL-341; GLU-341 AND PRO-385.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK000484 mRNA. Translation: BAA91196.1.
AL034380 Genomic DNA. Translation: CAB92120.1.
AL034380 Genomic DNA. Translation: CAI21625.1. Sequence problems.
AL034380 Genomic DNA. Translation: CAI21626.1. Sequence problems.
AL034380 Genomic DNA. Translation: CAI21627.1. Sequence problems.
CH471059 Genomic DNA. Translation: EAX07790.1.
CH471059 Genomic DNA. Translation: EAX07791.1.
CH471059 Genomic DNA. Translation: EAX07792.1.
BC013568 mRNA. Translation: AAH13568.1.
RefSeqNP_001189483.1. NM_001202554.1.
NP_060307.2. NM_017837.3.
UniGeneHs.259605.
Hs.732254.

3D structure databases

ProteinModelPortalQ9NUD9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120782. 2 interactions.
STRING9606.ENSP00000078527.

Protein family/group databases

CAZyGT76. Glycosyltransferase Family 76.

PTM databases

PhosphoSiteQ9NUD9.

Polymorphism databases

DMDM74752975.

Proteomic databases

PaxDbQ9NUD9.
PRIDEQ9NUD9.

Protocols and materials databases

DNASU55650.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000078527; ENSP00000078527; ENSG00000060642.
ENST00000374145; ENSP00000363260; ENSG00000060642.
GeneID55650.
KEGGhsa:55650.
UCSCuc001bmz.3. human.

Organism-specific databases

CTD55650.
GeneCardsGC01P027113.
H-InvDBHIX0159960.
HGNCHGNC:26031. PIGV.
MIM239300. phenotype.
610274. gene.
neXtProtNX_Q9NUD9.
Orphanet247262. Hyperphosphatasia-intellectual deficiency syndrome.
PharmGKBPA134952230.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5542.
HOGENOMHOG000232162.
HOVERGENHBG080592.
InParanoidQ9NUD9.
KOK07542.
OMAFLKYYEL.
OrthoDBEOG7VDXPB.
PhylomeDBQ9NUD9.
TreeFamTF314515.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00196.

Gene expression databases

ArrayExpressQ9NUD9.
BgeeQ9NUD9.
CleanExHS_PIGV.
GenevestigatorQ9NUD9.

Family and domain databases

InterProIPR007315. GPI_Mannosyltransferase_2.
[Graphical view]
PANTHERPTHR12468. PTHR12468. 1 hit.
PfamPF04188. Mannosyl_trans2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPIGV.
GenomeRNAi55650.
NextBio60346.
PROQ9NUD9.
SOURCESearch...

Entry information

Entry namePIGV_HUMAN
AccessionPrimary (citable) accession number: Q9NUD9
Secondary accession number(s): D3DPL2 expand/collapse secondary AC list , Q5JYG7, Q5JYG8, Q5JYG9, Q9NX26
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 98 of the entry and version 1 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