Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

GPI mannosyltransferase 3

Gene

Pigb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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

Pathway: 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

  • GPI anchor biosynthetic process Source: MGI
  • GPI anchor metabolic process Source: MGI
  • mannosylation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

GPI-anchor biosynthesis

Enzyme and pathway databases

ReactomeiREACT_336927. Synthesis of glycosylphosphatidylinositol (GPI).
UniPathwayiUPA00196.

Protein family/group databases

CAZyiGT22. Glycosyltransferase Family 22.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Pigb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1891825. Pigb.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei52 – 7221HelicalSequence AnalysisAdd
BLAST
Transmembranei125 – 14521HelicalSequence AnalysisAdd
BLAST
Transmembranei213 – 23321HelicalSequence AnalysisAdd
BLAST
Transmembranei244 – 26421HelicalSequence AnalysisAdd
BLAST
Transmembranei304 – 32421HelicalSequence AnalysisAdd
BLAST
Transmembranei327 – 34721HelicalSequence AnalysisAdd
BLAST
Transmembranei351 – 37121HelicalSequence AnalysisAdd
BLAST
Transmembranei376 – 39621HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: MGI
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 542542GPI mannosyltransferase 3PRO_0000246252Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi480 – 4801N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9JJQ0.
PaxDbiQ9JJQ0.
PRIDEiQ9JJQ0.

PTM databases

PhosphoSiteiQ9JJQ0.

Expressioni

Gene expression databases

BgeeiQ9JJQ0.
ExpressionAtlasiQ9JJQ0. baseline and differential.
GenevisibleiQ9JJQ0. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000096165.

Structurei

3D structure databases

ProteinModelPortaliQ9JJQ0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG276773.
GeneTreeiENSGT00550000075012.
HOGENOMiHOG000189846.
HOVERGENiHBG082136.
InParanoidiQ9JJQ0.
KOiK05286.
OMAiPYYSHIH.
OrthoDBiEOG761BV9.
PhylomeDBiQ9JJQ0.
TreeFamiTF313518.

Family and domain databases

InterProiIPR005599. GPI_mannosylTrfase.
[Graphical view]
PANTHERiPTHR22760. PTHR22760. 1 hit.
PfamiPF03901. Glyco_transf_22. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JJQ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESQAADYNP ASRNLHGSSG EMKLRRRKSR QYVSAQEKRS PRRGLLGENT
60 70 80 90 100
YLVLFTIALR ILNCFLVQTS FVPDEYWQSL EVAHRMVFSY GYLTWEWTER
110 120 130 140 150
LRGYTYPLIF ASIYKVLHLL GKDSVQFLIW IPRLGQALLS AVADIRLYSL
160 170 180 190 200
LKQLENQEVA QWVFLCQLCS WFTWYCCTRT LTNTMETSLT ALALFYYPLE
210 220 230 240 250
GSRSVNSVKY SLLVALACVV RPTALIPWVP LLFRHFYQEQ RKLHLTLHHF
260 270 280 290 300
LPVGFITFSL SLIIDRIFFG QWTLVQLNFL KFNVLQNLGT FYGSHPWHWY
310 320 330 340 350
LSQGFPVVLG THLPFFIHGC FLAPRRLHIL LLTVLWTLLV YSMLGHKEFR
360 370 380 390 400
FIYPVLPFCM VFCGYSLAHL KTWRKAALSF LLLSNVPLAF YTGLVHQRGT
410 420 430 440 450
LDVMNHIQKV CPRGPDPASA SVFIMMPCHS TPYYSHVHCP LSMRFLQCPP
460 470 480 490 500
DLTGKTQYLD EADMFYLNPL RWLQQEFHSN ASLPTHLVTF NVLEKEINTF
510 520 530 540
LTSGNYERAA TFFHTHWPER RTGSHIHVYE RRLPGRVNTG GN
Length:542
Mass (Da):63,120
Last modified:July 25, 2006 - v2
Checksum:iD426F71B01011437
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti208 – 2081V → I in BAA94827 (PubMed:8861954).Curated
Sequence conflicti407 – 4071I → V in AAH52658 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D84436 mRNA. Translation: BAA94827.1.
AK153819 mRNA. Translation: BAE32195.1.
BC052658 mRNA. Translation: AAH52658.1.
CCDSiCCDS40687.1.
RefSeqiNP_061377.2. NM_018889.3.
UniGeneiMm.139905.

Genome annotation databases

EnsembliENSMUST00000098566; ENSMUSP00000096165; ENSMUSG00000079469.
ENSMUST00000183746; ENSMUSP00000138885; ENSMUSG00000079469.
ENSMUST00000184035; ENSMUSP00000139269; ENSMUSG00000079469.
ENSMUST00000184389; ENSMUSP00000139076; ENSMUSG00000079469.
GeneIDi55981.
KEGGimmu:55981.
UCSCiuc009qqs.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D84436 mRNA. Translation: BAA94827.1.
AK153819 mRNA. Translation: BAE32195.1.
BC052658 mRNA. Translation: AAH52658.1.
CCDSiCCDS40687.1.
RefSeqiNP_061377.2. NM_018889.3.
UniGeneiMm.139905.

3D structure databases

ProteinModelPortaliQ9JJQ0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000096165.

Protein family/group databases

CAZyiGT22. Glycosyltransferase Family 22.

PTM databases

PhosphoSiteiQ9JJQ0.

Proteomic databases

MaxQBiQ9JJQ0.
PaxDbiQ9JJQ0.
PRIDEiQ9JJQ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000098566; ENSMUSP00000096165; ENSMUSG00000079469.
ENSMUST00000183746; ENSMUSP00000138885; ENSMUSG00000079469.
ENSMUST00000184035; ENSMUSP00000139269; ENSMUSG00000079469.
ENSMUST00000184389; ENSMUSP00000139076; ENSMUSG00000079469.
GeneIDi55981.
KEGGimmu:55981.
UCSCiuc009qqs.1. mouse.

Organism-specific databases

CTDi9488.
MGIiMGI:1891825. Pigb.

Phylogenomic databases

eggNOGiNOG276773.
GeneTreeiENSGT00550000075012.
HOGENOMiHOG000189846.
HOVERGENiHBG082136.
InParanoidiQ9JJQ0.
KOiK05286.
OMAiPYYSHIH.
OrthoDBiEOG761BV9.
PhylomeDBiQ9JJQ0.
TreeFamiTF313518.

Enzyme and pathway databases

UniPathwayiUPA00196.
ReactomeiREACT_336927. Synthesis of glycosylphosphatidylinositol (GPI).

Miscellaneous databases

NextBioi311682.
PROiQ9JJQ0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JJQ0.
ExpressionAtlasiQ9JJQ0. baseline and differential.
GenevisibleiQ9JJQ0. MM.

Family and domain databases

InterProiIPR005599. GPI_mannosylTrfase.
[Graphical view]
PANTHERiPTHR22760. PTHR22760. 1 hit.
PfamiPF03901. Glyco_transf_22. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Thymus.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Egg.

Entry informationi

Entry nameiPIGB_MOUSE
AccessioniPrimary (citable) accession number: Q9JJQ0
Secondary accession number(s): Q3U585, Q7TQ01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 25, 2006
Last modified: June 24, 2015
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.