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Protein

Phosphatidylinositol-glycan biosynthesis class X protein

Gene

PIGX

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Essential component of glycosylphosphatidylinositol-mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis. Probably acts by stabilizing the mannosyltransferase PIGM (By similarity).By similarity

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 - Biological processi

Complete GO annotation...

Keywords - Biological processi

GPI-anchor biosynthesis

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol-glycan biosynthesis class X protein
Short name:
PIG-X
Gene namesi
Name:PIGX
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:26046. PIGX.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 230209LumenalSequence analysisAdd
BLAST
Transmembranei231 – 25121HelicalSequence analysisAdd
BLAST
Topological domaini252 – 2587CytoplasmicSequence analysis

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134928970.

Polymorphism and mutation databases

BioMutaiPIGX.
DMDMi229463032.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 258237Phosphatidylinositol-glycan biosynthesis class X proteinPRO_0000246295Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi103 – 1031N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiQ8TBF5.
MaxQBiQ8TBF5.
PeptideAtlasiQ8TBF5.
PRIDEiQ8TBF5.

PTM databases

iPTMnetiQ8TBF5.
PhosphoSiteiQ8TBF5.

Expressioni

Gene expression databases

BgeeiQ8TBF5.
CleanExiHS_PIGX.
ExpressionAtlasiQ8TBF5. baseline and differential.
GenevisibleiQ8TBF5. HS.

Organism-specific databases

HPAiHPA029409.

Interactioni

Subunit structurei

Interacts with PIGM.By similarity

Protein-protein interaction databases

BioGridi120303. 2 interactions.

Family & Domainsi

Sequence similaritiesi

Belongs to the PIGX family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000015227.
HOVERGENiHBG060417.
InParanoidiQ8TBF5.
KOiK07541.
PhylomeDBiQ8TBF5.

Family and domain databases

InterProiIPR013233. PIG-X/PBN1.
[Graphical view]
PfamiPF08320. PIG-X. 1 hit.
[Graphical view]
SMARTiSM00780. PIG-X. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8TBF5-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAARVAAVRA AAWLLLGAAT GLTRGPAAAF TAARSDAGIR AMCSEIILRQ
60 70 80 90 100
EVLKDGFHRD LLIKVKFGES IEDLHTCRLL IKQDIPAGLY VDPYELASLR
110 120 130 140 150
ERNITEAVMV SENFDIEAPN YLSKESEVLI YARRDSQCID CFQAFLPVHC
160 170 180 190 200
RYHRPHSEDG EASIVVNNPD LLMFCDQEFP ILKCWAHSEV AAPCALENED
210 220 230 240 250
ICQWNKMKYK SVYKNVILQV PVGLTVHTSL VCSVTLLITI LCSTLILVAV

FKYGHFSL
Length:258
Mass (Da):28,788
Last modified:May 5, 2009 - v3
Checksum:i55D3B5A597E0B2E7
GO
Isoform 2 (identifier: Q8TBF5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     177-177: Q → QAGSRRMIRFRFDSFDKTI

Note: No experimental confirmation available.
Show »
Length:276
Mass (Da):30,974
Checksum:iA8A8A4739D308EE3
GO

Sequence cautioni

The sequence AAH22542.1 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence AAH22542.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA91233.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAA91233.1 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence BAA91233.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281A → T in AAH22542 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti155 – 1551P → L.
Corresponds to variant rs2291397 [ dbSNP | Ensembl ].
VAR_027035
Natural varianti197 – 1971E → D.1 Publication
Corresponds to variant rs17852091 [ dbSNP | Ensembl ].
VAR_027036

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei177 – 1771Q → QAGSRRMIRFRFDSFDKTI in isoform 2. 1 PublicationVSP_019842

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC055725 Genomic DNA. No translation available.
BC022542 mRNA. Translation: AAH22542.1. Sequence problems.
AK000529 mRNA. Translation: BAA91233.1. Sequence problems.
CCDSiCCDS3320.2. [Q8TBF5-1]
CCDS54701.1. [Q8TBF5-2]
RefSeqiNP_001159776.1. NM_001166304.1. [Q8TBF5-2]
NP_060331.3. NM_017861.3. [Q8TBF5-1]
UniGeneiHs.223296.

Genome annotation databases

EnsembliENST00000392391; ENSP00000376192; ENSG00000163964.
GeneIDi54965.
KEGGihsa:54965.
UCSCiuc003fwx.6. human. [Q8TBF5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC055725 Genomic DNA. No translation available.
BC022542 mRNA. Translation: AAH22542.1. Sequence problems.
AK000529 mRNA. Translation: BAA91233.1. Sequence problems.
CCDSiCCDS3320.2. [Q8TBF5-1]
CCDS54701.1. [Q8TBF5-2]
RefSeqiNP_001159776.1. NM_001166304.1. [Q8TBF5-2]
NP_060331.3. NM_017861.3. [Q8TBF5-1]
UniGeneiHs.223296.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120303. 2 interactions.

PTM databases

iPTMnetiQ8TBF5.
PhosphoSiteiQ8TBF5.

Polymorphism and mutation databases

BioMutaiPIGX.
DMDMi229463032.

Proteomic databases

EPDiQ8TBF5.
MaxQBiQ8TBF5.
PeptideAtlasiQ8TBF5.
PRIDEiQ8TBF5.

Protocols and materials databases

DNASUi54965.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000392391; ENSP00000376192; ENSG00000163964.
GeneIDi54965.
KEGGihsa:54965.
UCSCiuc003fwx.6. human. [Q8TBF5-1]

Organism-specific databases

CTDi54965.
GeneCardsiPIGX.
HGNCiHGNC:26046. PIGX.
HPAiHPA029409.
MIMi610276. gene.
neXtProtiNX_Q8TBF5.
PharmGKBiPA134928970.
GenAtlasiSearch...

Phylogenomic databases

HOGENOMiHOG000015227.
HOVERGENiHBG060417.
InParanoidiQ8TBF5.
KOiK07541.
PhylomeDBiQ8TBF5.

Enzyme and pathway databases

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

Miscellaneous databases

GenomeRNAii54965.
PROiQ8TBF5.
SOURCEiSearch...

Gene expression databases

BgeeiQ8TBF5.
CleanExiHS_PIGX.
ExpressionAtlasiQ8TBF5. baseline and differential.
GenevisibleiQ8TBF5. HS.

Family and domain databases

InterProiIPR013233. PIG-X/PBN1.
[Graphical view]
PfamiPF08320. PIG-X. 1 hit.
[Graphical view]
SMARTiSM00780. PIG-X. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "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), VARIANT ASP-197.
    Tissue: Brain.
  3. "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] OF 1-243 (ISOFORM 2).
  4. "Mammalian PIG-X and yeast Pbn1p are the essential components of glycosylphosphatidylinositol-mannosyltransferase I."
    Ashida H., Hong Y., Murakami Y., Shishioh N., Sugimoto N., Kim Y.U., Maeda Y., Kinoshita T.
    Mol. Biol. Cell 16:1439-1448(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION, IDENTIFICATION OF THE NON-CANONICAL START CODON.

Entry informationi

Entry nameiPIGX_HUMAN
AccessioniPrimary (citable) accession number: Q8TBF5
Secondary accession number(s): Q9NWZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: May 5, 2009
Last modified: July 6, 2016
This is version 103 of the entry and version 3 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 3
    Human chromosome 3: 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.