Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P57054 (PIGP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylinositol N-acetylglucosaminyltransferase subunit P

EC=2.4.1.198
Alternative name(s):
Down syndrome critical region protein 5
Down syndrome critical region protein C
Phosphatidylinositol-glycan biosynthesis class P protein
Short name=PIG-P
Gene names
Name:PIGP
Synonyms:DCRC, DSCR5, DSCRC
ORF Names:NPD010
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length158 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Part of the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis. Ref.3

Catalytic activity

UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol.

Pathway

Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.

Subunit structure

Associates with PIGA, PIGC, PIGH, PIGQ and DPM2. The latter is not essential for activity.

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Tissue specificity

Ubiquitous.

Sequence similarities

Belongs to the PIGP family.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform B (identifier: P57054-1)

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 A (identifier: P57054-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: Missing.
Isoform C (identifier: P57054-3)

Also known as: DCRC-S;

The sequence of this isoform differs from the canonical sequence as follows:
     1-50: Missing.
     51-52: FI → MV

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 158158Phosphatidylinositol N-acetylglucosaminyltransferase subunit P
PRO_0000191783

Regions

Transmembrane40 – 6021Helical; Potential
Transmembrane80 – 10021Helical; Potential

Natural variations

Alternative sequence1 – 5050Missing in isoform C.
VSP_004203
Alternative sequence1 – 2424Missing in isoform A.
VSP_004202
Alternative sequence51 – 522FI → MV in isoform C.
VSP_004204
Natural variant91A → T. Ref.1 Ref.2 Ref.4 Ref.6 Ref.9
Corresponds to variant rs2507733 [ dbSNP | Ensembl ].
VAR_061521
Natural variant1181Y → C.
Corresponds to variant rs16994704 [ dbSNP | Ensembl ].
VAR_050538
Natural variant1361R → S.
Corresponds to variant rs2276231 [ dbSNP | Ensembl ].
VAR_050539

Experimental info

Sequence conflict31P → S in BAA96872. Ref.1
Sequence conflict901I → V in BAA96873. Ref.1
Sequence conflict901I → V in AAF32289. Ref.2

Sequences

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

Last modified November 28, 2012. Version 3.
Checksum: 924CCEB84C9D2721

FASTA15818,059
        10         20         30         40         50         60 
MVPRSTSLAL IVFLFHRLSK APGKMVENSP SPLPERAIYG FVLFLSSQFG FILYLVWAFI 

        70         80         90        100        110        120 
PESWLNSLGL TYWPQKYWAV ALPVYLLIAI VIGYVLLFGI NMMSTSPLDS IHTITDNYAK 

       130        140        150 
NQQQKKYQEE AIPALRDISI SEVNQMFFLA AKELYTKN 

« Hide

Isoform A [UniParc].

Checksum: 47A2122FA663EB64
Show »

FASTA13415,408
Isoform C (DCRC-S) [UniParc].

Checksum: CF1E65158429EE48
Show »

FASTA10812,510

References

« Hide 'large scale' references
[1]"Isolation of two novel genes, DSCR5 and DSCR6, from Down syndrome critical region on human chromosome 21q22.2."
Shibuya K., Kudoh J., Minoshima S., Kawasaki K., Asakawa S., Shimizu N.
Biochem. Biophys. Res. Commun. 271:693-698(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C), VARIANT THR-9.
Tissue: Testis.
[2]"A novel gene, DSCR5, from the distal Down syndrome critical region on chromosome 21q22.2."
Togashi T., Choi D.-K., Taylor T.D., Suzuki Y., Sugano S., Hattori M., Sakaki Y.
DNA Res. 7:207-212(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C), VARIANT THR-9.
[3]"Initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-P and is regulated by DPM2."
Watanabe R., Murakami Y., Marmor M.D., Inoue N., Maeda Y., Hino J., Kangawa K., Julius M., Kinoshita T.
EMBO J. 19:4402-4411(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-33, FUNCTION (ISOFORM A).
[4]Song H., Gao G., Peng Y., Ren S., Chen Z., Han Z.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B), VARIANT THR-9.
Tissue: Pituitary.
[5]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
[6]"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] (ISOFORMS A AND B), VARIANT THR-9.
Tissue: Kidney and Umbilical cord blood.
[7]"Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. expand/collapse author list , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
[8]"The DNA sequence of human chromosome 21."
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. expand/collapse author list , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]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], VARIANT THR-9.
[10]"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 A).
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB037162 mRNA. Translation: BAA96871.1.
AB037163 mRNA. Translation: BAA96872.1.
AB037164 mRNA. Translation: BAA96873.1.
AB035742 mRNA. Translation: BAA95633.1.
AB035743 mRNA. Translation: BAA95634.1.
AB035744 mRNA. Translation: BAA95635.1.
AB035745 mRNA. Translation: BAA95636.1.
AF216305 mRNA. Translation: AAF32289.1.
AB039659 mRNA. Translation: BAB12395.1.
AF237812 mRNA. Translation: AAG09757.1.
BT007053 mRNA. Translation: AAP35702.1.
AK314457 mRNA. Translation: BAG37065.1.
AK316609 mRNA. Translation: BAG38196.1.
AB451328 mRNA. Translation: BAG70142.1.
AB451472 mRNA. Translation: BAG70286.1.
AP000704 Genomic DNA. No translation available.
AP001429 Genomic DNA. No translation available.
AP001431 Genomic DNA. No translation available.
AP001727 Genomic DNA. Translation: BAA95512.1.
CH471079 Genomic DNA. Translation: EAX09724.1.
CH471079 Genomic DNA. Translation: EAX09725.1.
CH471079 Genomic DNA. Translation: EAX09727.1.
CH471079 Genomic DNA. Translation: EAX09726.1.
CH471079 Genomic DNA. Translation: EAX09728.1.
BC005180 mRNA. Translation: AAH05180.1.
BC011007 mRNA. Translation: AAH11007.1.
CCDSCCDS13649.1. [P57054-1]
CCDS13650.1. [P57054-2]
PIRJC7301.
JC7302.
RefSeqNP_710148.1. NM_153681.2.
NP_710149.1. NM_153682.2. [P57054-2]
XP_005261047.1. XM_005260990.2. [P57054-2]
XP_006724073.1. XM_006724010.1. [P57054-2]
UniGeneHs.656565.
Hs.716087.

3D structure databases

ProteinModelPortalP57054.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119391. 4 interactions.
STRING9606.ENSP00000420037.

PTM databases

PhosphoSiteP57054.

Polymorphism databases

DMDM425906062.

Proteomic databases

PaxDbP57054.
PRIDEP57054.

Protocols and materials databases

DNASU51227.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360525; ENSP00000353719; ENSG00000185808. [P57054-2]
ENST00000399098; ENSP00000382049; ENSG00000185808. [P57054-3]
ENST00000399102; ENSP00000382053; ENSG00000185808. [P57054-2]
ENST00000399103; ENSP00000382054; ENSG00000185808. [P57054-2]
ENST00000464265; ENSP00000420037; ENSG00000185808. [P57054-1]
GeneID51227.
KEGGhsa:51227.
UCSCuc002yvw.1. human. [P57054-1]
uc002yvy.2. human. [P57054-3]

Organism-specific databases

CTD51227.
GeneCardsGC21M038435.
HGNCHGNC:3046. PIGP.
HPAHPA026921.
MIM605938. gene.
neXtProtNX_P57054.
PharmGKBPA27498.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG133279.
HOVERGENHBG000430.
InParanoidP57054.
KOK03861.
OMASEVNRMF.
OrthoDBEOG776SRZ.
PhylomeDBP57054.
TreeFamTF323799.

Enzyme and pathway databases

BRENDA2.4.1.198. 2681.
ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00196.

Gene expression databases

ArrayExpressP57054.
BgeeP57054.
CleanExHS_PIGP.
GenevestigatorP57054.

Family and domain databases

InterProIPR013717. PIG-P.
IPR016542. PIG-P_GPI19.
[Graphical view]
PfamPF08510. PIG-P. 1 hit.
[Graphical view]
PIRSFPIRSF008765. PIG-P_GPI19. 1 hit.
ProtoNetSearch...

Other

GeneWikiPIGP.
GenomeRNAi51227.
NextBio35535499.
PROP57054.
SOURCESearch...

Entry information

Entry namePIGP_HUMAN
AccessionPrimary (citable) accession number: P57054
Secondary accession number(s): B2RB18 expand/collapse secondary AC list , B2RE99, B5BU92, D3DSG7, J3KR75, Q53Y28, Q96KI1, Q9NZA6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 28, 2012
Last modified: July 9, 2014
This is version 112 of the entry and version 3 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 21

Human chromosome 21: entries, gene names and cross-references to MIM