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Protein

GPI mannosyltransferase 1

Gene

PIGM

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly.1 Publication

Pathwayi: glycosylphosphatidylinositol-anchor biosynthesis

This protein is involved in the pathway glycosylphosphatidylinositol-anchor biosynthesis, which is part of Glycolipid biosynthesis.
View all proteins of this organism that are known to be involved in the pathway glycosylphosphatidylinositol-anchor biosynthesis and in Glycolipid biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

GPI-anchor biosynthesis

Enzyme and pathway databases

ReactomeiR-HSA-162710. Synthesis of glycosylphosphatidylinositol (GPI).
UniPathwayiUPA00196.

Protein family/group databases

CAZyiGT50. Glycosyltransferase Family 50.

Names & Taxonomyi

Protein namesi
Recommended name:
GPI mannosyltransferase 1 (EC:2.4.1.-)
Alternative name(s):
GPI mannosyltransferase I
Short name:
GPI-MT-I
Phosphatidylinositol-glycan biosynthesis class M protein
Short name:
PIG-M
Gene namesi
Name:PIGM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:18858. PIGM.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1717CytoplasmicSequence analysisAdd
BLAST
Transmembranei18 – 3821HelicalSequence analysisAdd
BLAST
Topological domaini39 – 7941LumenalSequence analysisAdd
BLAST
Transmembranei80 – 10021HelicalSequence analysisAdd
BLAST
Topological domaini101 – 13838CytoplasmicSequence analysisAdd
BLAST
Transmembranei139 – 16123HelicalSequence analysisAdd
BLAST
Topological domaini162 – 1698LumenalSequence analysis
Transmembranei170 – 19021HelicalSequence analysisAdd
BLAST
Topological domaini191 – 22535CytoplasmicSequence analysisAdd
BLAST
Transmembranei226 – 24621HelicalSequence analysisAdd
BLAST
Topological domaini247 – 28741LumenalSequence analysisAdd
BLAST
Transmembranei288 – 30821HelicalSequence analysisAdd
BLAST
Topological domaini309 – 3146CytoplasmicSequence analysis
Transmembranei315 – 33723HelicalSequence analysisAdd
BLAST
Topological domaini338 – 3381LumenalSequence analysis
Transmembranei339 – 35012HelicalSequence analysisAdd
BLAST
Topological domaini351 – 3577CytoplasmicSequence analysis
Transmembranei358 – 37821HelicalSequence analysisAdd
BLAST
Topological domaini379 – 3846LumenalSequence analysis
Transmembranei385 – 40521HelicalSequence analysisAdd
BLAST
Topological domaini406 – 42318CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Glycosylphosphatidylinositol deficiency (GPID)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal recessive trait that results in a propensity to venous thrombosis and seizures. Deficiency is due to a point mutation in the regulatory sequences of PIGM that disrupts binding of the transcription factor SP1 to its cognate promoter motif, leading to a strong reduction of expression.
See also OMIM:610293

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi49 – 491D → A: Almost abolishes enzyme activity. 1 Publication
Mutagenesisi51 – 511D → A: Abolishes enzyme activity. 1 Publication

Organism-specific databases

MalaCardsiPIGM.
MIMi610293. phenotype.
Orphaneti83639. Hypercoagulability syndrome due to glycosylphosphatidylinositol deficiency.
PharmGKBiPA38718.

Polymorphism and mutation databases

BioMutaiPIGM.
DMDMi74752622.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 423423GPI mannosyltransferase 1PRO_0000246213Add
BLAST

Proteomic databases

MaxQBiQ9H3S5.
PaxDbiQ9H3S5.
PRIDEiQ9H3S5.

PTM databases

iPTMnetiQ9H3S5.
PhosphoSiteiQ9H3S5.

Expressioni

Gene expression databases

BgeeiQ9H3S5.
CleanExiHS_PIGM.
GenevisibleiQ9H3S5. HS.

Organism-specific databases

HPAiHPA047418.

Interactioni

Protein-protein interaction databases

BioGridi125010. 13 interactions.
IntActiQ9H3S5. 1 interaction.
STRINGi9606.ENSP00000357069.

Structurei

3D structure databases

ProteinModelPortaliQ9H3S5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PIGM family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3893. Eukaryota.
ENOG410XRDY. LUCA.
GeneTreeiENSGT00390000017728.
HOGENOMiHOG000186884.
HOVERGENiHBG082137.
InParanoidiQ9H3S5.
KOiK05284.
OMAiEFLEHTY.
OrthoDBiEOG7SBNQM.
PhylomeDBiQ9H3S5.
TreeFamiTF314752.

Family and domain databases

InterProiIPR007704. Mannosyltransferase_DXD.
[Graphical view]
PANTHERiPTHR12886. PTHR12886. 1 hit.
PfamiPF05007. Mannosyl_trans. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9H3S5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSTKHWGEW LLNLKVAPAG VFGVAFLARV ALVFYGVFQD RTLHVRYTDI
60 70 80 90 100
DYQVFTDAAR FVTEGRSPYL RATYRYTPLL GWLLTPNIYL SELFGKFLFI
110 120 130 140 150
SCDLLTAFLL YRLLLLKGLG RRQACGYCVF WLLNPLPMAV SSRGNADSIV
160 170 180 190 200
ASLVLMVLYL IKKRLVACAA VFYGFAVHMK IYPVTYILPI TLHLLPDRDN
210 220 230 240 250
DKSLRQFRYT FQACLYELLK RLCNRAVLLF VAVAGLTFFA LSFGFYYEYG
260 270 280 290 300
WEFLEHTYFY HLTRRDIRHN FSPYFYMLYL TAESKWSFSL GIAAFLPQLI
310 320 330 340 350
LLSAVSFAYY RDLVFCCFLH TSIFVTFNKV CTSQYFLWYL CLLPLVMPLV
360 370 380 390 400
RMPWKRAVVL LMLWFIGQAM WLAPAYVLEF QGKNTFLFIW LAGLFFLLIN
410 420
CSILIQIISH YKEEPLTERI KYD
Length:423
Mass (Da):49,460
Last modified:March 1, 2001 - v1
Checksum:iE17DCD8252E28EF0
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti365 – 3651F → L.
Corresponds to variant rs12409352 [ dbSNP | Ensembl ].
VAR_027026

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028127 mRNA. Translation: BAB18567.1.
AK074655 mRNA. Translation: BAC11116.1.
AL513302 Genomic DNA. Translation: CAH71492.1.
BC001803 mRNA. Translation: AAH01803.1.
BC019865 mRNA. Translation: AAH19865.1.
CCDSiCCDS1192.1.
RefSeqiNP_660150.1. NM_145167.2.
UniGeneiHs.552810.

Genome annotation databases

EnsembliENST00000368090; ENSP00000357069; ENSG00000143315.
GeneIDi93183.
KEGGihsa:93183.
UCSCiuc001fuv.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028127 mRNA. Translation: BAB18567.1.
AK074655 mRNA. Translation: BAC11116.1.
AL513302 Genomic DNA. Translation: CAH71492.1.
BC001803 mRNA. Translation: AAH01803.1.
BC019865 mRNA. Translation: AAH19865.1.
CCDSiCCDS1192.1.
RefSeqiNP_660150.1. NM_145167.2.
UniGeneiHs.552810.

3D structure databases

ProteinModelPortaliQ9H3S5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125010. 13 interactions.
IntActiQ9H3S5. 1 interaction.
STRINGi9606.ENSP00000357069.

Protein family/group databases

CAZyiGT50. Glycosyltransferase Family 50.

PTM databases

iPTMnetiQ9H3S5.
PhosphoSiteiQ9H3S5.

Polymorphism and mutation databases

BioMutaiPIGM.
DMDMi74752622.

Proteomic databases

MaxQBiQ9H3S5.
PaxDbiQ9H3S5.
PRIDEiQ9H3S5.

Protocols and materials databases

DNASUi93183.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368090; ENSP00000357069; ENSG00000143315.
GeneIDi93183.
KEGGihsa:93183.
UCSCiuc001fuv.2. human.

Organism-specific databases

CTDi93183.
GeneCardsiPIGM.
HGNCiHGNC:18858. PIGM.
HPAiHPA047418.
MalaCardsiPIGM.
MIMi610273. gene.
610293. phenotype.
neXtProtiNX_Q9H3S5.
Orphaneti83639. Hypercoagulability syndrome due to glycosylphosphatidylinositol deficiency.
PharmGKBiPA38718.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3893. Eukaryota.
ENOG410XRDY. LUCA.
GeneTreeiENSGT00390000017728.
HOGENOMiHOG000186884.
HOVERGENiHBG082137.
InParanoidiQ9H3S5.
KOiK05284.
OMAiEFLEHTY.
OrthoDBiEOG7SBNQM.
PhylomeDBiQ9H3S5.
TreeFamiTF314752.

Enzyme and pathway databases

UniPathwayiUPA00196.
ReactomeiR-HSA-162710. Synthesis of glycosylphosphatidylinositol (GPI).

Miscellaneous databases

ChiTaRSiPIGM. human.
GenomeRNAii93183.
NextBioi78019.
PROiQ9H3S5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H3S5.
CleanExiHS_PIGM.
GenevisibleiQ9H3S5. HS.

Family and domain databases

InterProiIPR007704. Mannosyltransferase_DXD.
[Graphical view]
PANTHERiPTHR12886. PTHR12886. 1 hit.
PfamiPF05007. Mannosyl_trans. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "PIG-M transfers the first mannose to glycosylphosphatidylinositol on the lumenal side of the ER."
    Maeda Y., Watanabe R., Harris C.L., Hong Y., Ohishi K., Kinoshita K., Kinoshita T.
    EMBO J. 20:250-261(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF ASP-49 AND ASP-51.
  2. "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].
    Tissue: Mammary gland.
  3. "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.
    , 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].
  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: Brain and Eye.
  5. Cited for: INVOLVEMENT IN GLYCOSYLPHOSPHATIDYLINOSITOL DEFICIENCY.

Entry informationi

Entry nameiPIGM_HUMAN
AccessioniPrimary (citable) accession number: Q9H3S5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: March 1, 2001
Last modified: March 16, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.