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P20933

- ASPG_HUMAN

UniProt

P20933 - ASPG_HUMAN

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Protein
N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase
Gene
AGA
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins.

Catalytic activityi

N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O = N-acetyl-beta-D-glucosaminylamine + L-aspartate.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei206 – 2061Nucleophile1 Publication

GO - Molecular functioni

  1. N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity Source: UniProtKB
  2. peptidase activity Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. protein deglycosylation Source: UniProtKB
  2. protein maturation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease

Enzyme and pathway databases

BRENDAi3.5.1.26. 2681.
SABIO-RKP20933.

Protein family/group databases

MEROPSiT02.001.

Names & Taxonomyi

Protein namesi
Recommended name:
N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase (EC:3.5.1.26)
Alternative name(s):
Aspartylglucosaminidase
Glycosylasparaginase
N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase
Cleaved into the following 2 chains:
Gene namesi
Name:AGA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:318. AGA.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
  3. lysosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Involvement in diseasei

Aspartylglucosaminuria (AGU) [MIM:208400]: An inborn lysosomal storage disease causing excess accumulation of glycoasparagine in the body tissues and its increased excretion in urine. Clinical features include mild to severe mental retardation manifesting from the age of two, coarse facial features and mild connective tissue abnormalities.
Note: The disease is caused by mutations affecting the gene represented in this entry.6 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121V → L in AGU; uncertain pathological significance. 1 Publication
Corresponds to variant rs74626221 [ dbSNP | Ensembl ].
VAR_015427
Natural varianti60 – 601G → D in AGU.
VAR_005069
Natural varianti72 – 721S → P in AGU; specifically prevents the proteolytic activation cleavage of AGA in the endoplasmic reticulum. 1 Publication
VAR_005070
Natural varianti100 – 1001G → E in AGU. 1 Publication
VAR_015428
Natural varianti101 – 1011A → V in AGU.
VAR_005071
Natural varianti135 – 1351F → S in AGU. 1 Publication
VAR_015429
Natural varianti161 – 1611R → Q in AGU. 3 Publications
Corresponds to variant rs192195150 [ dbSNP | Ensembl ].
VAR_005072
Natural varianti163 – 1631C → S in AGU; most frequent mutation; abolishes autocatalytic cleavage and enzyme activity. 3 Publications
Corresponds to variant rs121964904 [ dbSNP | Ensembl ].
VAR_005073
Natural varianti252 – 2521G → E in AGU. 1 Publication
VAR_015430
Natural varianti252 – 2521G → R in AGU. 1 Publication
VAR_015431
Natural varianti257 – 2571T → I in AGU. 1 Publication
VAR_015432
Natural varianti302 – 3021G → R in AGU.
VAR_005074
Natural varianti306 – 3061C → R in AGU.
VAR_005075

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi208400. phenotype.
Orphaneti93. Aspartylglucosaminuria.
PharmGKBiPA24615.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23231 Publication
Add
BLAST
Chaini24 – 205182Glycosylasparaginase alpha chain
PRO_0000002333Add
BLAST
Chaini206 – 346141Glycosylasparaginase beta chain
PRO_0000002334Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241Blocked amino end (Ser)
Glycosylationi38 – 381N-linked (GlcNAc...)3 Publications
Disulfide bondi64 ↔ 691 Publication
Disulfide bondi163 ↔ 1791 Publication
Disulfide bondi286 ↔ 3061 Publication
Glycosylationi308 – 3081N-linked (GlcNAc...)1 Publication
Disulfide bondi317 ↔ 3451 Publication

Post-translational modificationi

Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity.

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP20933.
PaxDbiP20933.
PRIDEiP20933.

PTM databases

PhosphoSiteiP20933.

Miscellaneous databases

PMAP-CutDBP20933.

Expressioni

Gene expression databases

ArrayExpressiP20933.
BgeeiP20933.
CleanExiHS_AGA.
GenevestigatoriP20933.

Organism-specific databases

HPAiHPA031415.
HPA031417.

Interactioni

Subunit structurei

Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers.1 Publication

Protein-protein interaction databases

BioGridi106683. 3 interactions.
IntActiP20933. 2 interactions.
STRINGi9606.ENSP00000264595.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 358
Helixi37 – 4812
Helixi53 – 6715
Helixi69 – 713
Beta strandi72 – 776
Beta strandi87 – 937
Turni94 – 963
Beta strandi99 – 1057
Beta strandi107 – 1093
Helixi111 – 12111
Beta strandi125 – 1284
Helixi129 – 13810
Helixi149 – 16012
Turni175 – 1773
Beta strandi207 – 2126
Beta strandi214 – 2163
Beta strandi218 – 2247
Turni241 – 2433
Beta strandi244 – 2485
Turni249 – 2513
Beta strandi252 – 2587
Helixi260 – 2634
Helixi264 – 2663
Helixi268 – 27710
Helixi282 – 29615
Beta strandi302 – 3087
Beta strandi313 – 3186
Beta strandi325 – 3317
Turni333 – 3353
Beta strandi339 – 3446

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1APYX-ray2.00A/C24-185[»]
B/D206-346[»]
1APZX-ray2.30A/C24-185[»]
B/D206-346[»]
ProteinModelPortaliP20933.
SMRiP20933. Positions 25-185, 206-346.

Miscellaneous databases

EvolutionaryTraceiP20933.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni234 – 2374Substrate binding
Regioni257 – 2604Substrate binding

Sequence similaritiesi

Belongs to the Ntn-hydrolase family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1446.
HOVERGENiHBG004289.
InParanoidiP20933.
KOiK01444.
OMAiKFFGAVI.
OrthoDBiEOG7RV9GJ.
PhylomeDBiP20933.
TreeFamiTF300756.

Family and domain databases

InterProiIPR029055. Ntn_hydrolases_N.
IPR000246. Peptidase_T2.
[Graphical view]
PANTHERiPTHR10188. PTHR10188. 1 hit.
PfamiPF01112. Asparaginase_2. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P20933-1 [UniParc]FASTAAdd to Basket

« Hide

MARKSNLPVL LVPFLLCQAL VRCSSPLPLV VNTWPFKNAT EAAWRALASG    50
GSALDAVESG CAMCEREQCD GSVGFGGSPD ELGETTLDAM IMDGTTMDVG 100
AVGDLRRIKN AIGVARKVLE HTTHTLLVGE SATTFAQSMG FINEDLSTTA 150
SQALHSDWLA RNCQPNYWRN VIPDPSKYCG PYKPPGILKQ DIPIHKETED 200
DRGHDTIGMV VIHKTGHIAA GTSTNGIKFK IHGRVGDSPI PGAGAYADDT 250
AGAAAATGNG DILMRFLPSY QAVEYMRRGE DPTIACQKVI SRIQKHFPEF 300
FGAVICANVT GSYGAACNKL STFTQFSFMV YNSEKNQPTE EKVDCI 346
Length:346
Mass (Da):37,208
Last modified:February 9, 2010 - v2
Checksum:i766F1690B5B62FFA
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121V → L in AGU; uncertain pathological significance. 1 Publication
Corresponds to variant rs74626221 [ dbSNP | Ensembl ].
VAR_015427
Natural varianti60 – 601G → D in AGU.
VAR_005069
Natural varianti72 – 721S → P in AGU; specifically prevents the proteolytic activation cleavage of AGA in the endoplasmic reticulum. 1 Publication
VAR_005070
Natural varianti100 – 1001G → E in AGU. 1 Publication
VAR_015428
Natural varianti101 – 1011A → V in AGU.
VAR_005071
Natural varianti135 – 1351F → S in AGU. 1 Publication
VAR_015429
Natural varianti149 – 1491T → S.8 Publications
Corresponds to variant rs2228119 [ dbSNP | Ensembl ].
VAR_033533
Natural varianti161 – 1611R → Q in AGU. 3 Publications
Corresponds to variant rs192195150 [ dbSNP | Ensembl ].
VAR_005072
Natural varianti163 – 1631C → S in AGU; most frequent mutation; abolishes autocatalytic cleavage and enzyme activity. 3 Publications
Corresponds to variant rs121964904 [ dbSNP | Ensembl ].
VAR_005073
Natural varianti252 – 2521G → E in AGU. 1 Publication
VAR_015430
Natural varianti252 – 2521G → R in AGU. 1 Publication
VAR_015431
Natural varianti257 – 2571T → I in AGU. 1 Publication
VAR_015432
Natural varianti302 – 3021G → R in AGU.
VAR_005074
Natural varianti306 – 3061C → R in AGU.
VAR_005075
Natural varianti322 – 3221T → I.
Corresponds to variant rs56849061 [ dbSNP | Ensembl ].
VAR_061026

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211V → A in AAB60655. 1 Publication
Sequence conflicti21 – 211V → A in CAA43958. 1 Publication
Sequence conflicti25 – 251S → C AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X55762 mRNA. Translation: CAA39288.1.
X55330 mRNA. Translation: CAA39029.1.
U21281
, U21273, U21274, U21275, U21277, U21278, U21279, U21280 Genomic DNA. Translation: AAB60655.1.
X61959 Genomic DNA. Translation: CAA43958.1.
M64073 mRNA. Translation: AAA35903.1.
M64075 mRNA. Translation: AAA35904.1. Sequence problems.
M64076 mRNA. Translation: AAA35905.1. Sequence problems.
M60808 mRNA. Translation: AAA35901.1.
M60809 mRNA. Translation: AAA35902.1.
AK312982 mRNA. Translation: BAG35819.1.
CR541715 mRNA. Translation: CAG46516.1.
AC078881 Genomic DNA. Translation: AAY40915.1.
AC027627 Genomic DNA. No translation available.
CH471056 Genomic DNA. Translation: EAX04714.1.
CH471056 Genomic DNA. Translation: EAX04715.1.
BC012392 mRNA. Translation: AAH12392.1.
CCDSiCCDS3829.1.
PIRiS11343. MUHUGD.
RefSeqiNP_000018.2. NM_000027.3.
NP_001165459.1. NM_001171988.1.
UniGeneiHs.207776.

Genome annotation databases

EnsembliENST00000264595; ENSP00000264595; ENSG00000038002.
GeneIDi175.
KEGGihsa:175.
UCSCiuc003iuu.2. human.

Polymorphism databases

DMDMi288558804.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X55762 mRNA. Translation: CAA39288.1 .
X55330 mRNA. Translation: CAA39029.1 .
U21281
, U21273 , U21274 , U21275 , U21277 , U21278 , U21279 , U21280 Genomic DNA. Translation: AAB60655.1 .
X61959 Genomic DNA. Translation: CAA43958.1 .
M64073 mRNA. Translation: AAA35903.1 .
M64075 mRNA. Translation: AAA35904.1 . Sequence problems.
M64076 mRNA. Translation: AAA35905.1 . Sequence problems.
M60808 mRNA. Translation: AAA35901.1 .
M60809 mRNA. Translation: AAA35902.1 .
AK312982 mRNA. Translation: BAG35819.1 .
CR541715 mRNA. Translation: CAG46516.1 .
AC078881 Genomic DNA. Translation: AAY40915.1 .
AC027627 Genomic DNA. No translation available.
CH471056 Genomic DNA. Translation: EAX04714.1 .
CH471056 Genomic DNA. Translation: EAX04715.1 .
BC012392 mRNA. Translation: AAH12392.1 .
CCDSi CCDS3829.1.
PIRi S11343. MUHUGD.
RefSeqi NP_000018.2. NM_000027.3.
NP_001165459.1. NM_001171988.1.
UniGenei Hs.207776.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1APY X-ray 2.00 A/C 24-185 [» ]
B/D 206-346 [» ]
1APZ X-ray 2.30 A/C 24-185 [» ]
B/D 206-346 [» ]
ProteinModelPortali P20933.
SMRi P20933. Positions 25-185, 206-346.
ModBasei Search...

Protein-protein interaction databases

BioGridi 106683. 3 interactions.
IntActi P20933. 2 interactions.
STRINGi 9606.ENSP00000264595.

Chemistry

BindingDBi P20933.

Protein family/group databases

MEROPSi T02.001.

PTM databases

PhosphoSitei P20933.

Polymorphism databases

DMDMi 288558804.

Proteomic databases

MaxQBi P20933.
PaxDbi P20933.
PRIDEi P20933.

Protocols and materials databases

DNASUi 175.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264595 ; ENSP00000264595 ; ENSG00000038002 .
GeneIDi 175.
KEGGi hsa:175.
UCSCi uc003iuu.2. human.

Organism-specific databases

CTDi 175.
GeneCardsi GC04M178351.
H-InvDB HIX0004652.
HGNCi HGNC:318. AGA.
HPAi HPA031415.
HPA031417.
MIMi 208400. phenotype.
613228. gene.
neXtProti NX_P20933.
Orphaneti 93. Aspartylglucosaminuria.
PharmGKBi PA24615.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1446.
HOVERGENi HBG004289.
InParanoidi P20933.
KOi K01444.
OMAi KFFGAVI.
OrthoDBi EOG7RV9GJ.
PhylomeDBi P20933.
TreeFami TF300756.

Enzyme and pathway databases

BRENDAi 3.5.1.26. 2681.
SABIO-RK P20933.

Miscellaneous databases

ChiTaRSi AGA. human.
EvolutionaryTracei P20933.
GeneWikii Aspartylglucosaminidase.
GenomeRNAii 175.
NextBioi 702.
PMAP-CutDB P20933.
PROi P20933.
SOURCEi Search...

Gene expression databases

ArrayExpressi P20933.
Bgeei P20933.
CleanExi HS_AGA.
Genevestigatori P20933.

Family and domain databases

InterProi IPR029055. Ntn_hydrolases_N.
IPR000246. Peptidase_T2.
[Graphical view ]
PANTHERi PTHR10188. PTHR10188. 1 hit.
Pfami PF01112. Asparaginase_2. 1 hit.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequence analysis of a cDNA for human glycosylasparaginase. A single gene encodes the subunits of this lysosomal amidase."
    Fisher K.J., Tollersrud O.-K., Aronson N.N. Jr.
    FEBS Lett. 269:440-444(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-149.
  2. Erratum
    Fisher K.J., Tollersrud O.-K., Aronson N.N. Jr.
    FEBS Lett. 276:232-232(1990) [PubMed] [Europe PMC] [Abstract]
  3. "Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease."
    Ikonen E., Baumann M., Groen K., Syvaenen A.-C., Enomaa N., Halila R., Aula P., Peltonen L.
    EMBO J. 10:51-58(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 206-235, ACTIVATION BY CLEAVAGE, CATALYTIC ACTIVITY, VARIANTS SER-149; AGU GLN-161 AND SER-163, CHARACTERIZATION OF VARIANT AGU SER-163.
    Tissue: Fetal liver.
  4. "Genomic structure of human lysosomal glycosylasparaginase."
    Park H., Fisher K.J., Aronson N.N. Jr.
    FEBS Lett. 288:168-172(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-149.
  5. "Characterization of the mutation responsible for aspartylglucosaminuria in three Finnish patients. Amino acid substitution Cys163-->Ser abolishes the activity of lysosomal glycosylasparaginase and its conversion into subunits."
    Fisher K.J., Aronson N.N. Jr.
    J. Biol. Chem. 266:12105-12113(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], AUTOCATALYTIC CLEAVAGE, CATALYTIC ACTIVITY, VARIANTS SER-149; AGU GLN-161 AND SER-163.
  6. "Aspartylglycosaminuria in the Finnish population: identification of two point mutations in the heavy chain of glycoasparaginase."
    Mononen I., Heisterkamp N., Kaartinen V., Williams J.C., Yates J.R. III, Griffin P.R., Hood L.E., Groffen J.
    Proc. Natl. Acad. Sci. U.S.A. 88:2941-2945(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-45; 47-60; 67-84; 98-120; 123-190; 206-314 AND 320-343, VARIANTS AGU GLN-161 AND SER-163.
  7. "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], VARIANT SER-149.
    Tissue: Urinary bladder.
  8. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-149.
  9. "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].
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-149.
  11. "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], VARIANT SER-149.
    Tissue: Ovary.
  12. "Purification and structure of human liver aspartylglucosaminidase."
    Rip J.W., Coulter-Mackie M.B., Rupar C.A., Gordon B.A.
    Biochem. J. 288:1005-1010(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-44 AND 206-231, GLYCOSYLATION AT ASN-38.
    Tissue: Liver.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Three-dimensional structure of human lysosomal aspartylglucosaminidase."
    Oinonen C., Tikkanen R., Rouvinen J., Peltonen L.
    Nat. Struct. Biol. 2:1102-1108(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 24-185 IN COMPLEX WITH ASPARTIC ACID, SUBUNIT, ACTIVE SITE, GLYCOSYLATION AT ASN-38 AND ASN-308, DISULFIDE BONDS.
  15. "Mutations causing aspartylglucosaminuria (AGU): a lysosomal accumulation disease."
    Ikonen E., Peltonen L.
    Hum. Mutat. 1:361-365(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON AGU VARIANTS.
  16. "Ser72-->Pro active-site disease mutation in human lysosomal aspartylglucosaminidase: abnormal intracellular processing and evidence for extracellular activation."
    Peltola M., Tikkanen R., Peltonen L., Jalanko A.
    Hum. Mol. Genet. 5:737-743(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT AGU PRO-72.
  17. "Two novel mutations in a Canadian family with aspartylglucosaminuria and early outcome post bone marrow transplantation."
    Laitinen A., Hietala M., Haworth J.C., Schroeder M.L., Seargeant L.E., Greenberg C.R., Aula P.
    Clin. Genet. 51:174-178(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS AGU GLU-100 AND SER-135.
  18. "Molecular pathogenesis of a disease: structural consequences of aspartylglucosaminuria mutations."
    Saarela J., Laine M., Oinonen C., Schantz C., Jalanko A., Rouvinen J., Peltonen L.
    Hum. Mol. Genet. 10:983-995(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS AGU LEU-12; ARG-252; GLU-252 AND ILE-257.

Entry informationi

Entry nameiASPG_HUMAN
AccessioniPrimary (citable) accession number: P20933
Secondary accession number(s): B2R7H2
, D3DP47, Q4W5Q2, Q6FHN6, Q9UCK6, Q9UCK7, Q9UCK8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 9, 2010
Last modified: September 3, 2014
This is version 152 of the entry and version 2 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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