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O95394

- AGM1_HUMAN

UniProt

O95394 - AGM1_HUMAN

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Protein

Phosphoacetylglucosamine mutase

Gene

PGM3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, a sugar nucleotide critical to multiple glycosylation pathways including protein N- and O-glycosylation.3 Publications

Catalytic activityi

N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate.3 Publications

Cofactori

Mg2+By similarityNote: Binds 1 Mg(2+) ion per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei64 – 641Phosphoserine intermediate1 Publication
Metal bindingi64 – 641Magnesium; via phosphate groupBy similarity
Metal bindingi276 – 2761MagnesiumBy similarity
Metal bindingi278 – 2781MagnesiumBy similarity
Metal bindingi280 – 2801MagnesiumBy similarity
Binding sitei505 – 5051SubstrateBy 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. glucosamine metabolic process Source: UniProtKB
  4. glucose 1-phosphate metabolic process Source: Ensembl
  5. hemopoiesis Source: RefGenome
  6. post-translational protein modification Source: Reactome
  7. protein N-linked glycosylation Source: UniProtKB
  8. protein N-linked glycosylation via asparagine Source: Reactome
  9. protein O-linked glycosylation Source: UniProtKB
  10. spermatogenesis Source: Ensembl
  11. UDP-N-acetylglucosamine biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism

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 mutaseCurated (EC:5.4.2.33 Publications)
Short name:
PAGM
Alternative name(s):
Acetylglucosamine phosphomutaseCurated
N-acetylglucosamine-phosphate mutase1 Publication
Phosphoglucomutase-3Imported
Short name:
PGM 3
Gene namesi
Name:PGM3Imported
Synonyms:AGM11 Publication
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
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Immunodeficiency 23 (IMD23) [MIM:615816]: A primary immunodeficiency syndrome characterized by recurrent respiratory and skin infections beginning in early childhood, severe atopy, increased serum IgE, and developmental delay or cognitive impairment of varying severity.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti83 – 831L → S in IMD23; decreased phosphoacetylglucosamine mutase activity; no effect on protein abundance. 1 Publication
VAR_071359
Natural varianti239 – 2391D → H in IMD23; decreased phosphoacetylglucosamine mutase activity. 1 Publication
VAR_071360
Natural varianti246 – 2461N → S in IMD23; loss of phosphoacetylglucosamine mutase activity. 1 Publication
VAR_071361
Natural varianti297 – 2971D → E in IMD23; decreased phosphoacetylglucosamine mutase activity; decreased protein abundance. 1 Publication
VAR_071362
Natural varianti340 – 3401Missing in IMD23; decreased phosphoacetylglucosamine mutase activity; decreased protein abundance. 1 Publication
VAR_071363
Natural varianti451 – 4511Q → R in IMD23; decreased phosphoacetylglucosamine mutase activity. 1 Publication
VAR_071364
Natural varianti501 – 5011E → Q in IMD23; decreased phosphoacetylglucosamine mutase activity; no effect on protein abundance. 1 Publication
VAR_071365
Natural varianti502 – 5021D → Y in IMD23; decreased phosphoacetylglucosamine mutase activity; no effect on protein abundance. 1 Publication
VAR_071366

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

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi615816. phenotype.
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.1 Publication

Gene expression databases

BgeeiO95394.
CleanExiHS_PGM3.
ExpressionAtlasiO95394. baseline and differential.
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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni370 – 3723Substrate bindingBy similarity
Regioni496 – 5005Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the phosphohexose mutase family.Curated

Phylogenomic databases

eggNOGiCOG1109.
GeneTreeiENSGT00390000000509.
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

        10         20         30         40         50
MDLGAITKYS ALHAKPNGLI LQYGTAGFRT KAEHLDHVMF RMGLLAVLRS
60 70 80 90 100
KQTKSTIGVM VTASHNPEED NGVKLVDPLG EMLAPSWEEH ATCLANAEEQ
110 120 130 140 150
DMQRVLIDIS EKEAVNLQQD AFVVIGRDTR PSSEKLSQSV IDGVTVLGGQ
160 170 180 190 200
FHDYGLLTTP QLHYMVYCRN TGGRYGKATI EGYYQKLSKA FVELTKQASC
210 220 230 240 250
SGDEYRSLKV DCANGIGALK LREMEHYFSQ GLSVQLFNDG SKGKLNHLCG
260 270 280 290 300
ADFVKSHQKP PQGMEIKSNE RCCSFDGDAD RIVYYYHDAD GHFHLIDGDK
310 320 330 340 350
IATLISSFLK ELLVEIGESL NIGVVQTAYA NGSSTRYLEE VMKVPVYCTK
360 370 380 390 400
TGVKHLHHKA QEFDIGVYFE ANGHGTALFS TAVEMKIKQS AEQLEDKKRK
410 420 430 440 450
AAKMLENIID LFNQAAGDAI SDMLVIEAIL ALKGLTVQQW DALYTDLPNR
460 470 480 490 500
QLKVQVADRR VISTTDAERQ AVTPPGLQEA INDLVKKYKL SRAFVRPSGT
510 520 530 540
EDVVRVYAEA DSQESADHLA HEVSLAVFQL AGGIGERPQP GF
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.Curated

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 varianti83 – 831L → S in IMD23; decreased phosphoacetylglucosamine mutase activity; no effect on protein abundance. 1 Publication
VAR_071359
Natural varianti239 – 2391D → H in IMD23; decreased phosphoacetylglucosamine mutase activity. 1 Publication
VAR_071360
Natural varianti246 – 2461N → S in IMD23; loss of phosphoacetylglucosamine mutase activity. 1 Publication
VAR_071361
Natural varianti297 – 2971D → E in IMD23; decreased phosphoacetylglucosamine mutase activity; decreased protein abundance. 1 Publication
VAR_071362
Natural varianti340 – 3401Missing in IMD23; decreased phosphoacetylglucosamine mutase activity; decreased protein abundance. 1 Publication
VAR_071363
Natural varianti451 – 4511Q → R in IMD23; decreased phosphoacetylglucosamine mutase activity. 1 Publication
VAR_071364
Natural varianti466 – 4661D → N in allele PGM3*2. 3 Publications
Corresponds to variant rs473267 [ dbSNP | Ensembl ].
VAR_013489
Natural varianti501 – 5011E → Q in IMD23; decreased phosphoacetylglucosamine mutase activity; no effect on protein abundance. 1 Publication
VAR_071365
Natural varianti502 – 5021D → Y in IMD23; decreased phosphoacetylglucosamine mutase activity; no effect on protein abundance. 1 Publication
VAR_071366

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
615816. phenotype.
neXtProti NX_O95394.
PharmGKBi PA33244.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1109.
GeneTreei ENSGT00390000000509.
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

ChiTaRSi PGM3. human.
GeneWikii Phosphoglucomutase_3.
GenomeRNAii 5238.
NextBioi 20236.
PROi O95394.
SOURCEi Search...

Gene expression databases

Bgeei O95394.
CleanExi HS_PGM3.
ExpressionAtlasi O95394. baseline and differential.
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

« Hide 'large scale' publications
  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), TISSUE SPECIFICITY.
  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, ACTIVE SITE, 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. Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INVOLVEMENT IN IMD23, VARIANTS IMD23 HIS-239; SER-246 AND ARG-451, CHARACTERIZATION OF VARIANTS IMD23 HIS-239; SER-246 AND ARG-451.
  17. "Autosomal recessive phosphoglucomutase 3 (PGM3) mutations link glycosylation defects to atopy, immune deficiency, autoimmunity, and neurocognitive impairment."
    Zhang Y., Yu X., Ichikawa M., Lyons J.J., Datta S., Lamborn I.T., Jing H., Kim E.S., Biancalana M., Wolfe L.A., DiMaggio T., Matthews H.F., Kranick S.M., Stone K.D., Holland S.M., Reich D.S., Hughes J.D., Mehmet H.
    , McElwee J., Freeman A.F., Freeze H.H., Su H.C., Milner J.D.
    J. Allergy Clin. Immunol. 133:1400-1409(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INVOLVEMENT IN IMD23, VARIANTS IMD23 GLU-297 AND GLN-501, CHARACTERIZATION OF VARIANTS IMD23 GLU-297 AND GLN-501.
  18. Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INVOLVEMENT IN IMD23, VARIANTS IMD23 SER-83; GLU-340 DEL AND TYR-502, CHARACTERIZATION OF VARIANTS IMD23 SER-83; GLU-340 DEL AND TYR-502.
  19. "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: November 26, 2014
This is version 154 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