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Q96IJ6

- GMPPA_HUMAN

UniProt

Q96IJ6 - GMPPA_HUMAN

Protein

Mannose-1-phosphate guanyltransferase alpha

Gene

GMPPA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    May serve as a regulatory subunit and allow allosteric feedback inhibition of GMPPB by GDP-mannose.1 Publication

    GO - Molecular functioni

    1. nucleotidyltransferase activity Source: InterPro

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. dolichol-linked oligosaccharide biosynthetic process Source: Reactome
    3. GDP-mannose biosynthetic process Source: Reactome
    4. post-translational protein modification Source: Reactome
    5. protein N-linked glycosylation via asparagine Source: Reactome

    Enzyme and pathway databases

    ReactomeiREACT_22423. Synthesis of GDP-mannose.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mannose-1-phosphate guanyltransferase alpha
    Alternative name(s):
    GDP-mannose pyrophosphorylase A
    Short name:
    GMPP-alpha
    GTP-mannose-1-phosphate guanylyltransferase alpha
    Gene namesi
    Name:GMPPA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:22923. GMPPA.

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: Myc-tagged GMPPA shows a diffuse cytoplasmic and nuclear pattern in transfected COS-7 cells.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Alacrima, achalasia, and mental retardation syndrome (AAMR) [MIM:615510]: An autosomal recessive disorder characterized by onset of alacrima, achalasia, and mental retardation at birth or in early infancy. More variable features include hypotonia, gait abnormalities, anisocoria, and visual or hearing deficits. The disorder shows similarity to the triple A syndrome, but patients with AAMR do not have adrenal insufficiency.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti182 – 1821G → D in AAMR; drastically reduced protein expression in fibroblasts and altered subcellular location; no effect on transferrin N-glycosylation profile. 1 Publication
    VAR_070203
    Natural varianti334 – 3341T → M in AAMR; no effect on transferrin N-glycosylation profile. 1 Publication
    VAR_070204
    Natural varianti334 – 3341T → P in AAMR; drastically reduced protein expression in fibroblasts, altered subcellular location and drastically increased GDP-mannose levels in lymphoblast; no effect on GDP-mannose pyrophosphorylase activity in lymphoblasts, nor on transferrin N-glycosylation profile. 1 Publication
    VAR_070205
    Natural varianti390 – 3901R → P in AAMR; drastically reduced protein expression in fibroblasts; no effect on transferrin N-glycosylation profile. 1 Publication
    VAR_070206
    Natural varianti401 – 4011N → T in AAMR; drastically reduced protein expression in fibroblasts and drastically increased GDP-mannose levels in lymphoblast; no effect on GDP-mannose pyrophosphorylase activity in lymphoblasts, nor on transferrin, IgG and total serum protein N-glycosylation profiles. 1 Publication
    VAR_070207

    Keywords - Diseasei

    Disease mutation, Mental retardation

    Organism-specific databases

    MIMi615510. phenotype.
    Orphaneti869. Triple A syndrome.
    PharmGKBiPA134925506.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 420420Mannose-1-phosphate guanyltransferase alphaPRO_0000327872Add
    BLAST

    Proteomic databases

    MaxQBiQ96IJ6.
    PaxDbiQ96IJ6.
    PRIDEiQ96IJ6.

    PTM databases

    PhosphoSiteiQ96IJ6.

    Expressioni

    Tissue specificityi

    Expressed in fibroblasts (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ96IJ6.
    BgeeiQ96IJ6.
    CleanExiHS_GMPPA.
    GenevestigatoriQ96IJ6.

    Organism-specific databases

    HPAiHPA035513.

    Interactioni

    Subunit structurei

    Associates with GMPPB.By similarity

    Protein-protein interaction databases

    BioGridi118967. 7 interactions.
    IntActiQ96IJ6. 3 interactions.
    MINTiMINT-3053969.
    STRINGi9606.ENSP00000315925.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96IJ6.
    SMRiQ96IJ6. Positions 4-416.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1208.
    HOVERGENiHBG059531.
    KOiK00966.
    OMAiGPRIRGN.
    OrthoDBiEOG7WHH9C.
    PhylomeDBiQ96IJ6.
    TreeFamiTF300832.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    InterProiIPR001451. Hexapep_transf.
    IPR018357. Hexapep_transf_CS.
    IPR005835. NTP_transferase.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view]
    PfamiPF00132. Hexapep. 1 hit.
    PF00483. NTP_transferase. 1 hit.
    [Graphical view]
    SUPFAMiSSF53448. SSF53448. 1 hit.
    PROSITEiPS00101. HEXAPEP_TRANSFERASES. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96IJ6-1) [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

    MLKAVILIGG PQKGTRFRPL SFEVPKPLFP VAGVPMIQHH IEACAQVPGM    50
    QEILLIGFYQ PDEPLTQFLE AAQQEFNLPV RYLQEFAPLG TGGGLYHFRD 100
    QILAGSPEAF FVLNADVCSD FPLSAMLEAH RRQRHPFLLL GTTANRTQSL 150
    NYGCIVENPQ THEVLHYVEK PSTFISDIIN CGIYLFSPEA LKPLRDVFQR 200
    NQQDGQLEDS PGLWPGAGTI RLEQDVFSAL AGQGQIYVHL TDGIWSQIKS 250
    AGSALYASRL YLSRYQDTHP ERLAKHTPGG PWIRGNVYIH PTAKVAPSAV 300
    LGPNVSIGKG VTVGEGVRLR ESIVLHGATL QEHTCVLHSI VGWGSTVGRW 350
    ARVEGTPSDP NPNDPRARMD SESLFKDGKL LPAITILGCR VRIPAEVLIL 400
    NSIVLPHKEL SRSFTNQIIL 420
    Length:420
    Mass (Da):46,291
    Last modified:December 1, 2001 - v1
    Checksum:i741B77ABA198D4BC
    GO
    Isoform 2 (identifier: Q96IJ6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         285-285: G → GTQPAPIPNLWLPPQPSEPGFLTSSPELKPQSLPLPDQIRFGIFAPRASLLLLG

    Show »
    Length:473
    Mass (Da):52,018
    Checksum:i0F283DF3FEA4C6E9
    GO

    Sequence cautioni

    The sequence AAD38517.1 differs from that shown. Reason: Frameshift at position 355.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti57 – 571G → C in BAD96671. 1 PublicationCurated
    Sequence conflicti67 – 671Q → H in BAF83360. (PubMed:14702039)Curated
    Sequence conflicti118 – 1181C → Y in BAA91460. (PubMed:14702039)Curated
    Sequence conflicti339 – 3391S → C in AAD38517. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti21 – 211S → F.
    Corresponds to variant rs34218609 [ dbSNP | Ensembl ].
    VAR_042434
    Natural varianti156 – 1561V → A.
    Corresponds to variant rs13396066 [ dbSNP | Ensembl ].
    VAR_042435
    Natural varianti182 – 1821G → D in AAMR; drastically reduced protein expression in fibroblasts and altered subcellular location; no effect on transferrin N-glycosylation profile. 1 Publication
    VAR_070203
    Natural varianti334 – 3341T → M in AAMR; no effect on transferrin N-glycosylation profile. 1 Publication
    VAR_070204
    Natural varianti334 – 3341T → P in AAMR; drastically reduced protein expression in fibroblasts, altered subcellular location and drastically increased GDP-mannose levels in lymphoblast; no effect on GDP-mannose pyrophosphorylase activity in lymphoblasts, nor on transferrin N-glycosylation profile. 1 Publication
    VAR_070205
    Natural varianti390 – 3901R → P in AAMR; drastically reduced protein expression in fibroblasts; no effect on transferrin N-glycosylation profile. 1 Publication
    VAR_070206
    Natural varianti401 – 4011N → T in AAMR; drastically reduced protein expression in fibroblasts and drastically increased GDP-mannose levels in lymphoblast; no effect on GDP-mannose pyrophosphorylase activity in lymphoblasts, nor on transferrin, IgG and total serum protein N-glycosylation profiles. 1 Publication
    VAR_070207

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei285 – 2851G → GTQPAPIPNLWLPPQPSEPG FLTSSPELKPQSLPLPDQIR FGIFAPRASLLLLG in isoform 2. CuratedVSP_032741

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF135422 mRNA. Translation: AAD38517.1. Frameshift.
    AK000999 mRNA. Translation: BAA91460.1.
    AK022578 mRNA. Translation: BAG51096.1.
    AK290671 mRNA. Translation: BAF83360.1.
    AK222951 mRNA. Translation: BAD96671.1.
    AC053503 Genomic DNA. Translation: AAY15053.1.
    CH471063 Genomic DNA. Translation: EAW70755.1.
    CH471063 Genomic DNA. Translation: EAW70759.1.
    BC007456 mRNA. Translation: AAH07456.1.
    CCDSiCCDS2441.1. [Q96IJ6-1]
    RefSeqiNP_037467.2. NM_013335.3. [Q96IJ6-1]
    NP_995319.1. NM_205847.2. [Q96IJ6-1]
    XP_005246543.1. XM_005246486.1. [Q96IJ6-1]
    UniGeneiHs.27059.

    Genome annotation databases

    EnsembliENST00000313597; ENSP00000315925; ENSG00000144591. [Q96IJ6-1]
    ENST00000341142; ENSP00000340760; ENSG00000144591. [Q96IJ6-1]
    ENST00000358215; ENSP00000350949; ENSG00000144591. [Q96IJ6-1]
    ENST00000373908; ENSP00000363016; ENSG00000144591. [Q96IJ6-1]
    ENST00000373917; ENSP00000363027; ENSG00000144591. [Q96IJ6-2]
    GeneIDi29926.
    KEGGihsa:29926.
    UCSCiuc002vlr.3. human. [Q96IJ6-1]

    Polymorphism databases

    DMDMi74732065.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF135422 mRNA. Translation: AAD38517.1 . Frameshift.
    AK000999 mRNA. Translation: BAA91460.1 .
    AK022578 mRNA. Translation: BAG51096.1 .
    AK290671 mRNA. Translation: BAF83360.1 .
    AK222951 mRNA. Translation: BAD96671.1 .
    AC053503 Genomic DNA. Translation: AAY15053.1 .
    CH471063 Genomic DNA. Translation: EAW70755.1 .
    CH471063 Genomic DNA. Translation: EAW70759.1 .
    BC007456 mRNA. Translation: AAH07456.1 .
    CCDSi CCDS2441.1. [Q96IJ6-1 ]
    RefSeqi NP_037467.2. NM_013335.3. [Q96IJ6-1 ]
    NP_995319.1. NM_205847.2. [Q96IJ6-1 ]
    XP_005246543.1. XM_005246486.1. [Q96IJ6-1 ]
    UniGenei Hs.27059.

    3D structure databases

    ProteinModelPortali Q96IJ6.
    SMRi Q96IJ6. Positions 4-416.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118967. 7 interactions.
    IntActi Q96IJ6. 3 interactions.
    MINTi MINT-3053969.
    STRINGi 9606.ENSP00000315925.

    PTM databases

    PhosphoSitei Q96IJ6.

    Polymorphism databases

    DMDMi 74732065.

    Proteomic databases

    MaxQBi Q96IJ6.
    PaxDbi Q96IJ6.
    PRIDEi Q96IJ6.

    Protocols and materials databases

    DNASUi 29926.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000313597 ; ENSP00000315925 ; ENSG00000144591 . [Q96IJ6-1 ]
    ENST00000341142 ; ENSP00000340760 ; ENSG00000144591 . [Q96IJ6-1 ]
    ENST00000358215 ; ENSP00000350949 ; ENSG00000144591 . [Q96IJ6-1 ]
    ENST00000373908 ; ENSP00000363016 ; ENSG00000144591 . [Q96IJ6-1 ]
    ENST00000373917 ; ENSP00000363027 ; ENSG00000144591 . [Q96IJ6-2 ]
    GeneIDi 29926.
    KEGGi hsa:29926.
    UCSCi uc002vlr.3. human. [Q96IJ6-1 ]

    Organism-specific databases

    CTDi 29926.
    GeneCardsi GC02P220327.
    HGNCi HGNC:22923. GMPPA.
    HPAi HPA035513.
    MIMi 615495. gene.
    615510. phenotype.
    neXtProti NX_Q96IJ6.
    Orphaneti 869. Triple A syndrome.
    PharmGKBi PA134925506.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1208.
    HOVERGENi HBG059531.
    KOi K00966.
    OMAi GPRIRGN.
    OrthoDBi EOG7WHH9C.
    PhylomeDBi Q96IJ6.
    TreeFami TF300832.

    Enzyme and pathway databases

    Reactomei REACT_22423. Synthesis of GDP-mannose.

    Miscellaneous databases

    GenomeRNAii 29926.
    NextBioi 52545.
    PROi Q96IJ6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96IJ6.
    Bgeei Q96IJ6.
    CleanExi HS_GMPPA.
    Genevestigatori Q96IJ6.

    Family and domain databases

    Gene3Di 3.90.550.10. 1 hit.
    InterProi IPR001451. Hexapep_transf.
    IPR018357. Hexapep_transf_CS.
    IPR005835. NTP_transferase.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view ]
    Pfami PF00132. Hexapep. 1 hit.
    PF00483. NTP_transferase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53448. SSF53448. 1 hit.
    PROSITEi PS00101. HEXAPEP_TRANSFERASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human homolog of GDP-mannose pyrophosphorylase."
      Matthijs G., Schollen E., Dierickx D.
      Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "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] (ISOFORM 1).
      Tissue: Embryo.
    3. 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] (ISOFORM 1).
      Tissue: Kidney.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Lymph.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: VARIANTS AAMR ASP-182; MET-334; PRO-334; PRO-390 AND THR-401, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiGMPPA_HUMAN
    AccessioniPrimary (citable) accession number: Q96IJ6
    Secondary accession number(s): A6NJ74
    , A8K3Q6, B3KMT4, Q53GI0, Q9NWC3, Q9Y5P5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 8, 2008
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 104 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

    Caution

    GMPPA is a close homolog of GMPPB, that has been shown to catalyze the formation of GDP-mannose, an essential precursor of glycan moieties of glycoproteins and glycolipids. However, lymphocytes from AAMR patients, that exhibit very low GMPPA protein levels, have unchanged GDP-mannose pyrophosphorylase activity and higher GDP-mannose levels than those from healthy controls. Affected individuals and control subjects show similar N-glycosylation profiles, both for transferrin glycosylation and for N-glycans derived from either total serum protein or immunoglobulin G. These observations led to the hypothesis that GMPPA might serve as a regulatory subunit and allow allosteric feedback inhibition of GMPPB by GDP-mannose. Alignment of GMPPAs and GMPPBs from various species shows that GMPPAs are characterized by a 2 amino acid-insertion (residues 11-12) in a highly conserved motif that borders the catalytic pocket and binds the nucleotide substrate in homologous enzymes. This insertion might inactivate the ancestral catalytic site, converting it to an allosteric site (PubMed:24035193).1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3