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Q96G03

- PGM2_HUMAN

UniProt

Q96G03 - PGM2_HUMAN

Protein

Phosphoglucomutase-2

Gene

PGM2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the conversion of the nucleoside breakdown products ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. May also catalyze the interconversion of glucose-1-phosphate and glucose-6-phosphate. Has low glucose 1,6-bisphosphate synthase activity.1 Publication

    Catalytic activityi

    Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.
    Alpha-D-ribose 1-phosphate = D-ribose 5-phosphate.
    2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy-alpha-D-ribose 5-phosphate.

    Cofactori

    Binds 1 magnesium ion per subunit.By similarity

    Kineticsi

    1. KM=45.7 µM for alpha-D-ribose 1-phosphate1 Publication
    2. KM=4.1 µM for 2-deoxy-alpha-D-ribose 1-phosphate1 Publication
    3. KM=114 µM for alpha-D-glucose 1-phosphate1 Publication

    Vmax=104.3 µmol/min/mg enzyme with alpha-D-ribose 1-phosphate as substrate1 Publication

    Vmax=20.8 µmol/min/mg enzyme with 2-deoxy-alpha-D-ribose 1-phosphate as substrate1 Publication

    Vmax=22.8 µmol/min/mg enzyme with alpha-D-glucose 1-phosphate as substrate1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei165 – 1651Phosphoserine intermediateBy similarity
    Metal bindingi165 – 1651Magnesium; via phosphate groupBy similarity
    Metal bindingi322 – 3221MagnesiumBy similarity
    Metal bindingi324 – 3241MagnesiumBy similarity
    Metal bindingi326 – 3261MagnesiumBy similarity

    GO - Molecular functioni

    1. magnesium ion binding Source: InterPro
    2. phosphoglucomutase activity Source: RefGenome
    3. phosphopentomutase activity Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. deoxyribose phosphate catabolic process Source: UniProtKB-UniPathway
    3. galactose catabolic process Source: RefGenome
    4. glucose metabolic process Source: RefGenome
    5. glycogen biosynthetic process Source: RefGenome
    6. glycogen catabolic process Source: Reactome
    7. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Carbohydrate metabolism, Glucose metabolism

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS09924-MONOMER.
    ReactomeiREACT_1008. Glycogen breakdown (glycogenolysis).
    REACT_169208. Glycogen synthesis.
    REACT_532. Galactose catabolism.
    SABIO-RKQ96G03.
    UniPathwayiUPA00002; UER00467.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoglucomutase-2 (EC:5.4.2.2)
    Short name:
    PGM 2
    Alternative name(s):
    Glucose phosphomutase 2
    Phosphodeoxyribomutase
    Phosphopentomutase (EC:5.4.2.7)
    Gene namesi
    Name:PGM2
    ORF Names:MSTP006
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:8906. PGM2.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytosol Source: RefGenome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33243.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 612611Phosphoglucomutase-2PRO_0000147781Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications
    Modified residuei165 – 1651Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ96G03.
    PaxDbiQ96G03.
    PeptideAtlasiQ96G03.
    PRIDEiQ96G03.

    PTM databases

    PhosphoSiteiQ96G03.

    Expressioni

    Gene expression databases

    ArrayExpressiQ96G03.
    BgeeiQ96G03.
    CleanExiHS_PGM2.
    GenevestigatoriQ96G03.

    Organism-specific databases

    HPAiHPA040676.

    Interactioni

    Protein-protein interaction databases

    BioGridi120564. 7 interactions.
    STRINGi9606.ENSP00000371393.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96G03.
    SMRiQ96G03. Positions 57-205.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the phosphohexose mutase family.Curated

    Phylogenomic databases

    eggNOGiCOG1109.
    HOGENOMiHOG000268676.
    HOVERGENiHBG056917.
    InParanoidiQ96G03.
    KOiK15779.
    OMAiRWDKNPL.
    OrthoDBiEOG715Q3R.
    PhylomeDBiQ96G03.
    TreeFamiTF300692.

    Family and domain databases

    Gene3Di3.30.310.50. 1 hit.
    3.40.120.10. 3 hits.
    InterProiIPR005844. A-D-PHexomutase_a/b/a-I.
    IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
    IPR005845. A-D-PHexomutase_a/b/a-II.
    IPR005846. A-D-PHexomutase_a/b/a-III.
    IPR005843. A-D-PHexomutase_C.
    IPR016066. A-D-PHexomutase_CS.
    IPR005841. Alpha-D-phosphohexomutase_SF.
    [Graphical view]
    PfamiPF02878. PGM_PMM_I. 1 hit.
    PF02879. PGM_PMM_II. 1 hit.
    PF02880. PGM_PMM_III. 1 hit.
    PF00408. PGM_PMM_IV. 1 hit.
    [Graphical view]
    PRINTSiPR00509. PGMPMM.
    SUPFAMiSSF53738. SSF53738. 3 hits.
    SSF55957. SSF55957. 1 hit.
    PROSITEiPS00710. PGM_PMM. 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. Align

    Isoform 1 (identifier: Q96G03-1) [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

    MAAPEGSGLG EDARLDQETA QWLRWDKNSL TLEAVKRLIA EGNKEELRKC    50
    FGARMEFGTA GLRAAMGPGI SRMNDLTIIQ TTQGFCRYLE KQFSDLKQKG 100
    IVISFDARAH PSSGGSSRRF ARLAATTFIS QGIPVYLFSD ITPTPFVPFT 150
    VSHLKLCAGI MITASHNPKQ DNGYKVYWDN GAQIISPHDK GISQAIEENL 200
    EPWPQAWDDS LIDSSPLLHN PSASINNDYF EDLKKYCFHR SVNRETKVKF 250
    VHTSVHGVGH SFVQSAFKAF DLVPPEAVPE QKDPDPEFPT VKYPNPEEGK 300
    GVLTLSFALA DKTKARIVLA NDPDADRLAV AEKQDSGEWR VFSGNELGAL 350
    LGWWLFTSWK EKNQDRSALK DTYMLSSTVS SKILRAIALK EGFHFEETLT 400
    GFKWMGNRAK QLIDQGKTVL FAFEEAIGYM CCPFVLDKDG VSAAVISAEL 450
    ASFLATKNLS LSQQLKAIYV EYGYHITKAS YFICHDQETI KKLFENLRNY 500
    DGKNNYPKAC GKFEISAIRD LTTGYDDSQP DKKAVLPTSK SSQMITFTFA 550
    NGGVATMRTS GTEPKIKYYA ELCAPPGNSD PEQLKKELNE LVSAIEEHFF 600
    QPQKYNLQPK AD 612
    Length:612
    Mass (Da):68,283
    Last modified:January 23, 2007 - v4
    Checksum:i82234DDE810D1F52
    GO
    Isoform 2 (identifier: Q96G03-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-8: MAAPEGSG → MSSQLILR
         9-147: Missing.
         429-430: YM → KK
         431-612: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:291
    Mass (Da):32,724
    Checksum:i743821357CF0B3A4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti114 – 1141G → A in BAD96957. 1 PublicationCurated
    Sequence conflicti162 – 1621I → V in BAA91938. 1 PublicationCurated
    Sequence conflicti282 – 2821K → R in CAB66640. (PubMed:11230166)Curated
    Sequence conflicti495 – 4951E → G in BAD96957. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti10 – 101G → D.2 Publications
    Corresponds to variant rs17856324 [ dbSNP | Ensembl ].
    VAR_027968
    Natural varianti488 – 4881E → D.
    Corresponds to variant rs10001580 [ dbSNP | Ensembl ].
    VAR_027969

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 88MAAPEGSG → MSSQLILR in isoform 2. 1 PublicationVSP_056221
    Alternative sequencei9 – 147139Missing in isoform 2. 1 PublicationVSP_056222Add
    BLAST
    Alternative sequencei429 – 4302YM → KK in isoform 2. 1 PublicationVSP_056223
    Alternative sequencei431 – 612182Missing in isoform 2. 1 PublicationVSP_056224Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL136705 mRNA. Translation: CAB66640.1.
    AF109360 mRNA. Translation: AAQ13508.1.
    AK001845 mRNA. Translation: BAA91938.1.
    AK303374 mRNA. Translation: BAG64430.1.
    CR457274 mRNA. Translation: CAG33555.1.
    AK223237 mRNA. Translation: BAD96957.1.
    AC021106 Genomic DNA. No translation available.
    AC108022 Genomic DNA. No translation available.
    BC010087 mRNA. Translation: AAH10087.1.
    CCDSiCCDS3443.1.
    RefSeqiNP_060760.2. NM_018290.3.
    UniGeneiHs.23363.
    Hs.607816.

    Genome annotation databases

    EnsembliENST00000381967; ENSP00000371393; ENSG00000169299.
    ENST00000544359; ENSP00000438025; ENSG00000169299.
    GeneIDi55276.
    KEGGihsa:55276.
    UCSCiuc011byb.1. human.

    Polymorphism databases

    DMDMi116242708.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL136705 mRNA. Translation: CAB66640.1 .
    AF109360 mRNA. Translation: AAQ13508.1 .
    AK001845 mRNA. Translation: BAA91938.1 .
    AK303374 mRNA. Translation: BAG64430.1 .
    CR457274 mRNA. Translation: CAG33555.1 .
    AK223237 mRNA. Translation: BAD96957.1 .
    AC021106 Genomic DNA. No translation available.
    AC108022 Genomic DNA. No translation available.
    BC010087 mRNA. Translation: AAH10087.1 .
    CCDSi CCDS3443.1.
    RefSeqi NP_060760.2. NM_018290.3.
    UniGenei Hs.23363.
    Hs.607816.

    3D structure databases

    ProteinModelPortali Q96G03.
    SMRi Q96G03. Positions 57-205.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120564. 7 interactions.
    STRINGi 9606.ENSP00000371393.

    PTM databases

    PhosphoSitei Q96G03.

    Polymorphism databases

    DMDMi 116242708.

    Proteomic databases

    MaxQBi Q96G03.
    PaxDbi Q96G03.
    PeptideAtlasi Q96G03.
    PRIDEi Q96G03.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000381967 ; ENSP00000371393 ; ENSG00000169299 .
    ENST00000544359 ; ENSP00000438025 ; ENSG00000169299 .
    GeneIDi 55276.
    KEGGi hsa:55276.
    UCSCi uc011byb.1. human.

    Organism-specific databases

    CTDi 55276.
    GeneCardsi GC04P037828.
    HGNCi HGNC:8906. PGM2.
    HPAi HPA040676.
    MIMi 172000. gene.
    neXtProti NX_Q96G03.
    PharmGKBi PA33243.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1109.
    HOGENOMi HOG000268676.
    HOVERGENi HBG056917.
    InParanoidi Q96G03.
    KOi K15779.
    OMAi RWDKNPL.
    OrthoDBi EOG715Q3R.
    PhylomeDBi Q96G03.
    TreeFami TF300692.

    Enzyme and pathway databases

    UniPathwayi UPA00002 ; UER00467 .
    BioCyci MetaCyc:HS09924-MONOMER.
    Reactomei REACT_1008. Glycogen breakdown (glycogenolysis).
    REACT_169208. Glycogen synthesis.
    REACT_532. Galactose catabolism.
    SABIO-RK Q96G03.

    Miscellaneous databases

    GeneWikii PGM2.
    GenomeRNAii 55276.
    NextBioi 59409.
    PROi Q96G03.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96G03.
    Bgeei Q96G03.
    CleanExi HS_PGM2.
    Genevestigatori Q96G03.

    Family and domain databases

    Gene3Di 3.30.310.50. 1 hit.
    3.40.120.10. 3 hits.
    InterProi IPR005844. A-D-PHexomutase_a/b/a-I.
    IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
    IPR005845. A-D-PHexomutase_a/b/a-II.
    IPR005846. A-D-PHexomutase_a/b/a-III.
    IPR005843. A-D-PHexomutase_C.
    IPR016066. A-D-PHexomutase_CS.
    IPR005841. Alpha-D-phosphohexomutase_SF.
    [Graphical view ]
    Pfami PF02878. PGM_PMM_I. 1 hit.
    PF02879. PGM_PMM_II. 1 hit.
    PF02880. PGM_PMM_III. 1 hit.
    PF00408. PGM_PMM_IV. 1 hit.
    [Graphical view ]
    PRINTSi PR00509. PGMPMM.
    SUPFAMi SSF53738. SSF53738. 3 hits.
    SSF55957. SSF55957. 1 hit.
    PROSITEi PS00710. PGM_PMM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Kidney.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Aorta.
    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] (ISOFORMS 1 AND 2).
      Tissue: Thymus.
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ASP-10.
    5. 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: Gastric mucosa.
    6. "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].
    7. "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-10.
      Tissue: Muscle.
    8. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-14, ACETYLATION AT ALA-2.
      Tissue: Platelet.
    9. "Molecular identification of mammalian phosphopentomutase and glucose-1,6-bisphosphate synthase, two members of the alpha-D-phosphohexomutase family."
      Maliekal P., Sokolova T., Vertommen D., Veiga-da-Cunha M., Van Schaftingen E.
      J. Biol. Chem. 282:31844-31851(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPGM2_HUMAN
    AccessioniPrimary (citable) accession number: Q96G03
    Secondary accession number(s): B4E0G8
    , Q53FP5, Q5QTR0, Q9H0P9, Q9NV22
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 122 of the entry and version 4 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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

    External Data

    Dasty 3