Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O95394

- AGM1_HUMAN

UniProt

O95394 - AGM1_HUMAN

Protein

Phosphoacetylglucosamine mutase

Gene

PGM3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Interconverts GlcNAc-6-P and GlcNAc-1-P.

    Catalytic activityi

    N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate.

    Cofactori

    Binds 1 magnesium ion per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei64 – 641Phosphoserine intermediate
    Metal bindingi64 – 641Magnesium; via phosphate groupBy similarity
    Metal bindingi276 – 2761MagnesiumBy similarity
    Metal bindingi278 – 2781MagnesiumBy similarity
    Metal bindingi280 – 2801MagnesiumBy similarity

    GO - Molecular functioni

    1. magnesium ion binding Source: InterPro
    2. phosphoacetylglucosamine mutase activity Source: UniProtKB
    3. phosphoglucomutase activity Source: Ensembl

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. dolichol-linked oligosaccharide biosynthetic process Source: Reactome
    3. embryo development Source: Ensembl
    4. glucosamine metabolic process Source: UniProtKB
    5. glucose 1-phosphate metabolic process Source: Ensembl
    6. hemopoiesis Source: RefGenome
    7. post-translational protein modification Source: Reactome
    8. protein N-linked glycosylation via asparagine Source: Reactome
    9. spermatogenesis Source: Ensembl
    10. UDP-N-acetylglucosamine biosynthetic process Source: RefGenome

    Keywords - Molecular functioni

    Isomerase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS00347-MONOMER.
    BRENDAi5.4.2.3. 2681.
    ReactomeiREACT_22394. Synthesis of UDP-N-acetyl-glucosamine.
    SABIO-RKO95394.
    UniPathwayiUPA00113; UER00530.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoacetylglucosamine mutase (EC:5.4.2.3)
    Short name:
    PAGM
    Alternative name(s):
    Acetylglucosamine phosphomutase
    N-acetylglucosamine-phosphate mutase
    Phosphoglucomutase-3
    Short name:
    PGM 3
    Gene namesi
    Name:PGM3
    Synonyms:AGM1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:8907. PGM3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: RefGenome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi64 – 641S → A: Loss of activity. 1 Publication
    Mutagenesisi65 – 651H → A: Loss of activity. 1 Publication
    Mutagenesisi278 – 2781D → A or E: Loss of activity. 1 Publication
    Mutagenesisi281 – 2811R → A or K: Loss of activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA33244.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 542542Phosphoacetylglucosamine mutasePRO_0000148013Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei64 – 641Phosphoserine3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO95394.
    PaxDbiO95394.
    PRIDEiO95394.

    PTM databases

    PhosphoSiteiO95394.

    Expressioni

    Tissue specificityi

    Found in many tissues except lung. Relatively high expression in pancreas, heart, liver, and placenta, and relatively low expression in brain, skeletal muscle and kidney.

    Gene expression databases

    ArrayExpressiO95394.
    BgeeiO95394.
    CleanExiHS_PGM3.
    GenevestigatoriO95394.

    Organism-specific databases

    HPAiCAB004998.
    HPA029759.
    HPA029760.

    Interactioni

    Protein-protein interaction databases

    BioGridi111257. 7 interactions.
    IntActiO95394. 1 interaction.
    MINTiMINT-5000376.

    Structurei

    3D structure databases

    ProteinModelPortaliO95394.
    SMRiO95394. Positions 5-540.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the phosphohexose mutase family.Curated

    Phylogenomic databases

    eggNOGiCOG1109.
    HOVERGENiHBG024321.
    InParanoidiO95394.
    KOiK01836.
    OMAiDIVRVYA.
    OrthoDBiEOG7W6WKJ.
    PhylomeDBiO95394.
    TreeFamiTF105670.

    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.
    IPR005843. A-D-PHexomutase_C.
    IPR016066. A-D-PHexomutase_CS.
    IPR016657. PAGM.
    [Graphical view]
    PfamiPF02878. PGM_PMM_I. 2 hits.
    PF02879. PGM_PMM_II. 1 hit.
    PF00408. PGM_PMM_IV. 1 hit.
    [Graphical view]
    PIRSFiPIRSF016408. PAGM. 1 hit.
    SUPFAMiSSF53738. SSF53738. 3 hits.
    SSF55957. SSF55957. 1 hit.
    PROSITEiPS00710. PGM_PMM. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95394-1) [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

    MDLGAITKYS ALHAKPNGLI LQYGTAGFRT KAEHLDHVMF RMGLLAVLRS    50
    KQTKSTIGVM VTASHNPEED NGVKLVDPLG EMLAPSWEEH ATCLANAEEQ 100
    DMQRVLIDIS EKEAVNLQQD AFVVIGRDTR PSSEKLSQSV IDGVTVLGGQ 150
    FHDYGLLTTP QLHYMVYCRN TGGRYGKATI EGYYQKLSKA FVELTKQASC 200
    SGDEYRSLKV DCANGIGALK LREMEHYFSQ GLSVQLFNDG SKGKLNHLCG 250
    ADFVKSHQKP PQGMEIKSNE RCCSFDGDAD RIVYYYHDAD GHFHLIDGDK 300
    IATLISSFLK ELLVEIGESL NIGVVQTAYA NGSSTRYLEE VMKVPVYCTK 350
    TGVKHLHHKA QEFDIGVYFE ANGHGTALFS TAVEMKIKQS AEQLEDKKRK 400
    AAKMLENIID LFNQAAGDAI SDMLVIEAIL ALKGLTVQQW DALYTDLPNR 450
    QLKVQVADRR VISTTDAERQ AVTPPGLQEA INDLVKKYKL SRAFVRPSGT 500
    EDVVRVYAEA DSQESADHLA HEVSLAVFQL AGGIGERPQP GF 542
    Length:542
    Mass (Da):59,852
    Last modified:May 1, 1999 - v1
    Checksum:i6A4FBCD99A2154A9
    GO
    Isoform 2 (identifier: O95394-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         542-542: F → YKAAETTHNINNAFGPGTANEHTVP

    Note: Gene prediction based on EST data.

    Show »
    Length:566
    Mass (Da):62,342
    Checksum:i81691708BD389ECF
    GO
    Isoform 3 (identifier: O95394-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MGGEWGQSAICPESAQEWTYQVGQHLVDM

    Note: No experimental confirmation available.

    Show »
    Length:570
    Mass (Da):62,941
    Checksum:i3F59B307C746CF8D
    GO

    Sequence cautioni

    The sequence BAB14652.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51A → V in BAG63306. (PubMed:14702039)Curated
    Sequence conflicti70 – 701D → G in BAG63306. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti466 – 4661D → N in allele PGM3*2. 3 Publications
    Corresponds to variant rs473267 [ dbSNP | Ensembl ].
    VAR_013489

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MGGEWGQSAICPESAQEWTY QVGQHLVDM in isoform 3. 1 PublicationVSP_047319
    Alternative sequencei542 – 5421F → YKAAETTHNINNAFGPGTAN EHTVP in isoform 2. CuratedVSP_047320

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF102265 mRNA. Translation: AAC72409.1.
    AF180371 mRNA. Translation: AAD55097.1.
    AB032081 mRNA. Translation: BAB00613.1.
    AK023709 mRNA. Translation: BAB14652.1. Different initiation.
    AK301867 mRNA. Translation: BAG63306.1.
    AK314512 mRNA. Translation: BAG37112.1.
    AL049699 Genomic DNA. No translation available.
    AL121716 Genomic DNA. No translation available.
    CH471051 Genomic DNA. Translation: EAW48670.1.
    CH471051 Genomic DNA. Translation: EAW48671.1.
    BC001258 mRNA. Translation: AAH01258.1.
    AL117443 mRNA. Translation: CAB55928.1.
    CCDSiCCDS4997.1. [O95394-1]
    CCDS56435.1. [O95394-3]
    CCDS56436.1. [O95394-4]
    PIRiT17238.
    RefSeqiNP_001186846.1. NM_001199917.1. [O95394-4]
    NP_001186848.1. NM_001199919.1. [O95394-3]
    NP_056414.1. NM_015599.2. [O95394-1]
    XP_006715567.1. XM_006715504.1. [O95394-4]
    UniGeneiHs.661665.

    Genome annotation databases

    EnsembliENST00000506587; ENSP00000425809; ENSG00000013375. [O95394-4]
    ENST00000512866; ENSP00000421565; ENSG00000013375. [O95394-3]
    ENST00000513973; ENSP00000424874; ENSG00000013375. [O95394-1]
    GeneIDi5238.
    KEGGihsa:5238.
    UCSCiuc003pju.2. human. [O95394-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF102265 mRNA. Translation: AAC72409.1 .
    AF180371 mRNA. Translation: AAD55097.1 .
    AB032081 mRNA. Translation: BAB00613.1 .
    AK023709 mRNA. Translation: BAB14652.1 . Different initiation.
    AK301867 mRNA. Translation: BAG63306.1 .
    AK314512 mRNA. Translation: BAG37112.1 .
    AL049699 Genomic DNA. No translation available.
    AL121716 Genomic DNA. No translation available.
    CH471051 Genomic DNA. Translation: EAW48670.1 .
    CH471051 Genomic DNA. Translation: EAW48671.1 .
    BC001258 mRNA. Translation: AAH01258.1 .
    AL117443 mRNA. Translation: CAB55928.1 .
    CCDSi CCDS4997.1. [O95394-1 ]
    CCDS56435.1. [O95394-3 ]
    CCDS56436.1. [O95394-4 ]
    PIRi T17238.
    RefSeqi NP_001186846.1. NM_001199917.1. [O95394-4 ]
    NP_001186848.1. NM_001199919.1. [O95394-3 ]
    NP_056414.1. NM_015599.2. [O95394-1 ]
    XP_006715567.1. XM_006715504.1. [O95394-4 ]
    UniGenei Hs.661665.

    3D structure databases

    ProteinModelPortali O95394.
    SMRi O95394. Positions 5-540.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111257. 7 interactions.
    IntActi O95394. 1 interaction.
    MINTi MINT-5000376.

    PTM databases

    PhosphoSitei O95394.

    Proteomic databases

    MaxQBi O95394.
    PaxDbi O95394.
    PRIDEi O95394.

    Protocols and materials databases

    DNASUi 5238.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000506587 ; ENSP00000425809 ; ENSG00000013375 . [O95394-4 ]
    ENST00000512866 ; ENSP00000421565 ; ENSG00000013375 . [O95394-3 ]
    ENST00000513973 ; ENSP00000424874 ; ENSG00000013375 . [O95394-1 ]
    GeneIDi 5238.
    KEGGi hsa:5238.
    UCSCi uc003pju.2. human. [O95394-1 ]

    Organism-specific databases

    CTDi 5238.
    GeneCardsi GC06M083876.
    HGNCi HGNC:8907. PGM3.
    HPAi CAB004998.
    HPA029759.
    HPA029760.
    MIMi 172100. gene.
    neXtProti NX_O95394.
    PharmGKBi PA33244.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1109.
    HOVERGENi HBG024321.
    InParanoidi O95394.
    KOi K01836.
    OMAi DIVRVYA.
    OrthoDBi EOG7W6WKJ.
    PhylomeDBi O95394.
    TreeFami TF105670.

    Enzyme and pathway databases

    UniPathwayi UPA00113 ; UER00530 .
    BioCyci MetaCyc:HS00347-MONOMER.
    BRENDAi 5.4.2.3. 2681.
    Reactomei REACT_22394. Synthesis of UDP-N-acetyl-glucosamine.
    SABIO-RK O95394.

    Miscellaneous databases

    GeneWikii Phosphoglucomutase_3.
    GenomeRNAii 5238.
    NextBioi 20236.
    PROi O95394.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95394.
    Bgeei O95394.
    CleanExi HS_PGM3.
    Genevestigatori O95394.

    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.
    IPR005843. A-D-PHexomutase_C.
    IPR016066. A-D-PHexomutase_CS.
    IPR016657. PAGM.
    [Graphical view ]
    Pfami PF02878. PGM_PMM_I. 2 hits.
    PF02879. PGM_PMM_II. 1 hit.
    PF00408. PGM_PMM_IV. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF016408. PAGM. 1 hit.
    SUPFAMi SSF53738. SSF53738. 3 hits.
    SSF55957. SSF55957. 1 hit.
    PROSITEi PS00710. PGM_PMM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Matthijs G., Schollen E., Dierickx D.
      Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Cloning and characterization of complementary DNA encoding human N-acetylglucosamine-phosphate mutase protein."
      Li C., Rodriguez M., Banerjee D.
      Gene 242:97-103(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Functional cloning and mutational analysis of the human cDNA for phosphoacetylglucosamine mutase: identification of the amino acid residues essential for the catalysis."
      Mio T., Yamada-Okabe T., Arisawa M., Yamada-Okabe H.
      Biochim. Biophys. Acta 1492:369-376(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS, VARIANT ASN-466.
    4. "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 3).
      Tissue: Placenta and Testis.
    5. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. 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 ASN-466.
      Tissue: Placenta.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 392-542 (ISOFORM 1).
      Tissue: Testis.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Identification of human phosphoglucomutase 3 (PGM3) as N-acetylglucosamine-phosphate mutase (AGM1)."
      Pang H., Koda Y., Soejima M., Kimura H.
      Ann. Hum. Genet. 66:139-144(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ASN-466.

    Entry informationi

    Entry nameiAGM1_HUMAN
    AccessioniPrimary (citable) accession number: O95394
    Secondary accession number(s): B2RB65
    , B4DX94, D6RF12, E1P547, E9PF86, Q5JWR4, Q96J46, Q9H8G5, Q9NS94, Q9NTT6, Q9UFV5, Q9UIY2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 152 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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