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Reviewed, UniProtKB/Swiss-Prot Q92521 (PIGB_HUMAN)

Last modified April 14, 2009. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    GPI mannosyltransferase 3
    EC=2.4.1.-
Alternative name(s):
    GPI mannosyltransferase III
      Short name=GPI-MT-III
    Phosphatidylinositol-glycan biosynthesis class B protein
      Short name=PIG-B
Gene names
Name: PIGB
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length554 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the third alpha-1,2-mannose to Man2-GlcN-acyl-PI during GPI precursor assembly. Ref.1

Pathway

Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Ref.1

Sequence similarities

Belongs to the glycosyltransferase 22 family. PIGB subfamily.

Ontologies

Keywords
   Biological processGPI-anchor biosynthesis
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
Gene Ontology (GO)
   Biological processpreassembly of GPI anchor in ER membrane

Inferred from Experiment. Source: Reactome

   Cellular componentintegral to membrane Ref.1

Non-traceable author statement. Source: UniProtKB

intrinsic to endoplasmic reticulum membrane

Inferred from electronic annotation. Source: InterPro

   Molecular functionglycolipid mannosyltransferase activity Ref.1

Inferred from Experiment. Source: Reactome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 554554GPI mannosyltransferase 3
PRO_0000246251

Regions

Transmembrane63 – 8321 Potential
Transmembrane136 – 15621 Potential
Transmembrane192 – 21221 Potential
Transmembrane224 – 24421 Potential
Transmembrane255 – 27521 Potential
Transmembrane315 – 33521 Potential
Transmembrane340 – 36021 Potential
Transmembrane362 – 38221 Potential
Transmembrane387 – 40721 Potential

Amino acid modifications

Glycosylation261N-linked (GlcNAc...) Potential
Glycosylation4271N-linked (GlcNAc...) Potential

Natural variations

Natural variant681I → L: dbSNP rs17851556. Ref.2
VAR_027027
Natural variant1621M → T: dbSNP rs2290344.
VAR_027028
Natural variant2991W → L: dbSNP rs678892. Ref.2 Ref.3
VAR_027029
Natural variant4841L → S: dbSNP rs17851554. Ref.2
VAR_027030
Natural variant5021S → G: dbSNP rs652397.
VAR_049224
Natural variant5511K → T: dbSNP rs2444042.
VAR_027031

Experimental info

Sequence conflict1981T → I in BAD97050. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q92521-1 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: B2AF87D13ADF90B3

FASTA55465,056
        10         20         30         40         50         60 
MRRPLSKCGM EPGGGDASLT LHGLQNRSHG KIKLRKRKST LYFNTQEKSA RRRGDLLGEN 

        70         80         90        100        110        120 
IYLLLFTIAL RILNCFLVQT SFVPDEYWQS LEVSHHMVFN YGYLTWEWTE RLRSYTYPLI 

       130        140        150        160        170        180 
FASIYKILHL LGKDSVQLLI WIPRLAQALL SAVADVRLYS LMKQLENQEV ARWVFFCQLC 

       190        200        210        220        230        240 
SWFTWYCCTR TLTNTMETVL TIIALFYYPL EGSKSMNSVK YSSLVALAFI IRPTAVILWT 

       250        260        270        280        290        300 
PLLFRHFCQE PRKLDLILHH FLPVGFVTLS LSLMIDRIFF GQWTLVQFNF LKFNVLQNWG 

       310        320        330        340        350        360 
TFYGSHPWHW YFSQGFPVIL GTHLPFFIHG CYLAPKRYRI LLVTVLWTLL VYSMLSHKEF 

       370        380        390        400        410        420 
RFIYPVLPFC MVFCGYSLTH LKTWKKPALS FLFLSNLFLA LYTGLVHQRG TLDVMSHIQK 

       430        440        450        460        470        480 
VCYNNPNKSS ASIFIMMPCH STPYYSHVHC PLPMRFLQCP PDLTGKSHYL DEADVFYLNP 

       490        500        510        520        530        540 
LNWLHREFHD DASLPTHLIT FSILEEEISA FLISSNYKRT AVFFHTHLPE GRIGSHIYVY 

       550 
ERKLKGKFNM KMKF 

« Hide

References

« Hide 'large scale' references
[1]"PIG-B, a membrane protein of the endoplasmic reticulum with a large lumenal domain, is involved in transferring the third mannose of the GPI anchor."
Takahashi M., Inoue N., Ohishi K., Maeda Y., Nakamura N., Endo Y., Fujita T., Takeda J., Kinoshita T.
EMBO J. 15:4254-4261(1996) [PubMed: 8861954] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
[2]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS LEU-68; LEU-299 AND SER-484.
Tissue: Testis.
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LEU-299.
Tissue: Prostate.
[4]"Glycoinositol phospholipid anchor-defective K562 mutants with biochemical lesions distinct from those in Thy-1- murine lymphoma mutants."
Mohney R.P., Knez J.J., Ravi L., Sevlever D., Rosenberry T.L., Hirose S., Medof M.E.
J. Biol. Chem. 269:6536-6542(1994) [PubMed: 7907094] [Abstract]
Cited for: IDENTIFICATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

D42138 mRNA. Translation: BAA07709.1.
AK223330 mRNA. Translation: BAD97050.1.
BC017711 mRNA. Translation: AAH17711.1.
IPIIPI00145121.
PIRS71751.
RefSeqNP_004846.4.
UniGeneHs.612814

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyGT22. Glycosyltransferase Family 22.

PTM databases

PhosphoSiteQ92521.

Proteomic databases

PRIDEQ92521.

Genome annotation databases

EnsemblENSG00000069943. Homo sapiens. [Contig view]
GeneID9488.
KEGGhsa:9488.

Organism-specific databases

GeneCardsGC15P053398.
H-InvDBHIX0012262.
HGNCHGNC:8959. PIGB.
MIM604122. gene.
PharmGKBPA33290.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ92521.
HOVERGENQ92521.

Enzyme and pathway databases

ReactomeREACT_1069. Post-translational protein modification.

Gene expression databases

ArrayExpressQ92521.
BgeeQ92521.
CleanExHS_PIGB.
GermOnlineENSG00000069943. Homo sapiens.

Family and domain databases

InterProIPR005599. Alg9_trans.
[Graphical view]
PANTHERPTHR22760. Alg9_trans. 1 hit.
PfamPF03901. Glyco_transf_22. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio35552.
SOURCESearch...

Entry information

Entry namePIGB_HUMAN
AccessionPrimary (citable) accession number: Q92521
Secondary accession number(s): Q53FF9, Q8WVN7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: February 1, 1997
Last modified: April 14, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents