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Protein

N-acetylglucosamine-1-phosphotransferase subunits alpha/beta

Gene

GNPTAB

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

Functioni

Catalyzes the formation of mannose 6-phosphate (M6P) markers on high mannose type oligosaccharides in the Golgi apparatus. M6P residues are required to bind to the M6P receptors (MPR), which mediate the vesicular transport of lysosomal enzymes to the endosomal/prelysosomal compartment.2 Publications

Catalytic activityi

UDP-N-acetyl-D-glucosamine + lysosomal-enzyme D-mannose = UMP + lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi449 – 4491CalciumPROSITE-ProRule annotation
Metal bindingi464 – 4641CalciumPROSITE-ProRule annotation
Metal bindingi467 – 4671CalciumPROSITE-ProRule annotation
Metal bindingi516 – 5161CalciumPROSITE-ProRule annotation
Metal bindingi531 – 5311CalciumPROSITE-ProRule annotation
Metal bindingi534 – 5341CalciumPROSITE-ProRule annotation
Sitei928 – 9292Cleavage; by MBTPS1

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi1018 – 102912PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • carbohydrate phosphorylation Source: UniProtKB
  • cell differentiation Source: InterPro
  • lysosome organization Source: UniProtKB
  • N-glycan processing to lysosome Source: UniProtKB
  • protein secretion Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi2.7.8.17. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetylglucosamine-1-phosphotransferase subunits alpha/beta (EC:2.7.8.171 Publication)
Alternative name(s):
GlcNAc-1-phosphotransferase subunits alpha/beta
Stealth protein GNPTAB
UDP-N-acetylglucosamine-1-phosphotransferase subunits alpha/beta
Cleaved into the following 2 chains:
Gene namesi
Name:GNPTAB
Synonyms:GNPTA, KIAA1208
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:29670. GNPTAB.

Subcellular locationi

N-acetylglucosamine-1-phosphotransferase subunit alpha :
N-acetylglucosamine-1-phosphotransferase subunit beta :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei22 – 4221HelicalSequence AnalysisAdd
BLAST
Transmembranei1215 – 123521HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • Golgi apparatus Source: UniProtKB
  • Golgi membrane Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • nucleus Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Mucolipidosis type II (MLII)13 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionFatal, autosomal recessive, lysosomal storage disorder characterized by severe clinical and radiologic features, peculiar fibroblast inclusions, and no excessive mucopolysacchariduria. Congenital dislocation of the hip, thoracic deformities, hernia, and hyperplastic gums are evident soon after birth.

See also OMIM:252500
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti4 – 41K → Q in MLIIIA; also found in patients with intermediate phenotype between MLII and MLIIIA; no effect on protein abundance; decreased retention in the Golgi; mistargeted to lysosomes and plasma membrane; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 6 Publications
Corresponds to variant rs34159654 [ dbSNP | Ensembl ].
VAR_027509
Natural varianti15 – 151S → Y in MLIIIA; unknown pathological significance; no effect on protein abundance; decreased protein cleavage into alpha and beta subunits; decreased retention in the Golgi; mistargeted to lysosomes and plasma membrane; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 3 Publications
VAR_073124
Natural varianti81 – 811W → L in MLII; no effect on protein abundance; decreased localization to the Golgi; defects in protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 3 Publications
VAR_070831
Natural varianti182 – 1821V → D in MLII; unknown pathological significance; decreased localization to the Golgi; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_073125
Natural varianti190 – 1901D → V in MLIIIA; also found in patients with intermediate phenotype between MLII and MLIIIA; unknown pathological significance; no effect on protein abundance; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 1 Publication
Corresponds to variant rs34946266 [ dbSNP | Ensembl ].
VAR_053545
Natural varianti205 – 2051Q → P in MLII; unknown pathological significance. 1 Publication
VAR_073126
Natural varianti334 – 3341R → L in MLII; no effect on protein abundance; loss of localization to the Golgi; loss of protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_073127
Natural varianti334 – 3341R → Q in MLIIIA; no effect on protein abundance; loss of localization to the Golgi; loss of protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_073128
Natural varianti348 – 3481I → L in MLII; unknown pathological significance; no effect on protein abundance; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
Corresponds to variant rs7958709 [ dbSNP | Ensembl ].
VAR_027510
Natural varianti374 – 3741F → L in MLII and MLIIIA; no effect on protein abundance; no effect on localization to the Golgi; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_062807
Natural varianti399 – 3991S → F in MLIIIA; no effect on protein abundance; loss of localization to the Golgi; defects in protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 5 Publications
VAR_062808
Natural varianti403 – 4031I → T in MLIIIA; no effect on protein abundance; loss of localization to the Golgi; loss of protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 3 Publications
VAR_062809
Natural varianti407 – 4071D → A in MLIIIA; no effect on protein abundance; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_025416
Natural varianti442 – 4421C → Y in MLIIIA; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity toward some substrates. 2 Publications
VAR_062810
Natural varianti461 – 4611C → G in MLIIIA; no effect on protein abundance; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity toward some substrates. 2 Publications
VAR_062811
Natural varianti468 – 4681C → S in MLIIIA; patients with intermediate phenotype between MLII and MLIIIA; no effect on protein abundance; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity toward some substrates. 2 Publications
VAR_073129
Natural varianti505 – 5051C → Y in MLIIIA; unknown pathological significance; decreased localization to the Golgi; decreased protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 3 Publications
VAR_070832
Natural varianti587 – 5871R → P in MLIIIA; decreased localization to the Golgi; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_073131
Natural varianti732 – 7321K → N in MLII; no effect on localization to the Golgi; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity toward some substrates. 3 Publications
VAR_070833
Natural varianti926 – 9261Q → P in MLIIIA; no effect on localization to the Golgi; loss of protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_062812
Natural varianti928 – 9281K → R in MLII; unknown pathological significance. 1 Publication
VAR_073134
Natural varianti955 – 9551A → V in MLII; unknown pathological significance; no effect on protein abundance; no effect on localization to the Golgi; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_073135
Natural varianti956 – 9561H → R in MLIIIA; unknown pathological significance. 1 Publication
VAR_073136
Natural varianti956 – 9561H → Y in MLIIIA; no effect on protein abundance; no effect on localization to the Golgi. 2 Publications
VAR_062813
Natural varianti986 – 9861R → C in MLII; decreased protein abundance; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 4 Publications
VAR_070834
Natural varianti1001 – 10011L → P in MLII; no effect on protein abundance; decreased localization to the Golgi; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_062814
Natural varianti1018 – 10181D → G in MLIIIA; patients with intermediate phenotype between MLII and MLIIIA; unknown pathological significance; no effect on protein abundance; decreased localization to the Golgi; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_073137
Natural varianti1054 – 10541L → V in MLII; unknown pathological significance; no effect on localization to the Golgi; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_073138
Natural varianti1153 – 11531N → S in MLIIIA; no effect on protein abundance; no effect on localization to the Golgi; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_062815
Natural varianti1236 – 12361K → M in MLII; decreased protein abundance; no effect on localization to the Golgi; does not suppress protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 3 Publications
VAR_027511
Mucolipidosis type III complementation group A (MLIIIA)13 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAutosomal recessive disease of lysosomal enzyme targeting. Clinically MLIII is characterized by restricted joint mobility, skeletal dysplasia, and short stature. Mildly coarsened facial features and thickening of the skin have been described. Cardiac valvular disease and corneal clouding may also occur. Half of the reported patients show learning disabilities or mental retardation.

See also OMIM:252600
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti4 – 41K → Q in MLIIIA; also found in patients with intermediate phenotype between MLII and MLIIIA; no effect on protein abundance; decreased retention in the Golgi; mistargeted to lysosomes and plasma membrane; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 6 Publications
Corresponds to variant rs34159654 [ dbSNP | Ensembl ].
VAR_027509
Natural varianti15 – 151S → Y in MLIIIA; unknown pathological significance; no effect on protein abundance; decreased protein cleavage into alpha and beta subunits; decreased retention in the Golgi; mistargeted to lysosomes and plasma membrane; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 3 Publications
VAR_073124
Natural varianti190 – 1901D → V in MLIIIA; also found in patients with intermediate phenotype between MLII and MLIIIA; unknown pathological significance; no effect on protein abundance; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 1 Publication
Corresponds to variant rs34946266 [ dbSNP | Ensembl ].
VAR_053545
Natural varianti334 – 3341R → Q in MLIIIA; no effect on protein abundance; loss of localization to the Golgi; loss of protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_073128
Natural varianti374 – 3741F → L in MLII and MLIIIA; no effect on protein abundance; no effect on localization to the Golgi; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_062807
Natural varianti399 – 3991S → F in MLIIIA; no effect on protein abundance; loss of localization to the Golgi; defects in protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 5 Publications
VAR_062808
Natural varianti403 – 4031I → T in MLIIIA; no effect on protein abundance; loss of localization to the Golgi; loss of protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 3 Publications
VAR_062809
Natural varianti407 – 4071D → A in MLIIIA; no effect on protein abundance; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_025416
Natural varianti442 – 4421C → Y in MLIIIA; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity toward some substrates. 2 Publications
VAR_062810
Natural varianti461 – 4611C → G in MLIIIA; no effect on protein abundance; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity toward some substrates. 2 Publications
VAR_062811
Natural varianti468 – 4681C → S in MLIIIA; patients with intermediate phenotype between MLII and MLIIIA; no effect on protein abundance; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity toward some substrates. 2 Publications
VAR_073129
Natural varianti505 – 5051C → Y in MLIIIA; unknown pathological significance; decreased localization to the Golgi; decreased protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 3 Publications
VAR_070832
Natural varianti587 – 5871R → P in MLIIIA; decreased localization to the Golgi; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_073131
Natural varianti926 – 9261Q → P in MLIIIA; no effect on localization to the Golgi; loss of protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_062812
Natural varianti956 – 9561H → R in MLIIIA; unknown pathological significance. 1 Publication
VAR_073136
Natural varianti956 – 9561H → Y in MLIIIA; no effect on protein abundance; no effect on localization to the Golgi. 2 Publications
VAR_062813
Natural varianti1018 – 10181D → G in MLIIIA; patients with intermediate phenotype between MLII and MLIIIA; unknown pathological significance; no effect on protein abundance; decreased localization to the Golgi; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_073137
Natural varianti1153 – 11531N → S in MLIIIA; no effect on protein abundance; no effect on localization to the Golgi; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_062815

Defects in GNPTAB have been suggested to play a role in susceptibility to persistent stuttering. Stuttering is a common speech disorder characterized by repetitions, prolongations, and interruptions in the flow of speech.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi925 – 9251R → A: Abolishes proteolytic cleavage by MBTPS1. 1 Publication
Mutagenesisi927 – 9271L → A: Abolishes proteolytic cleavage by MBTPS1. 1 Publication
Mutagenesisi928 – 9281K → A: Abolishes proteolytic cleavage by MBTPS1. 1 Publication

Keywords - Diseasei

Disease mutation, Mucolipidosis

Organism-specific databases

MIMi252500. phenotype.
252600. phenotype.
Orphaneti576. Mucolipidosis type 2.
577. Mucolipidosis type 3.
PharmGKBiPA128394710.

Polymorphism and mutation databases

BioMutaiGNPTAB.
DMDMi90185244.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 928928N-acetylglucosamine-1-phosphotransferase subunit alphaPRO_0000225008Add
BLAST
Chaini929 – 1256328N-acetylglucosamine-1-phosphotransferase subunit betaPRO_0000225009Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi83 – 831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi114 – 1141N-linked (GlcNAc...)Sequence Analysis
Glycosylationi148 – 1481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi179 – 1791N-linked (GlcNAc...)Sequence Analysis
Glycosylationi250 – 2501N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi438 ↔ 461PROSITE-ProRule annotation
Disulfide bondi452 ↔ 468PROSITE-ProRule annotation
Disulfide bondi505 ↔ 528PROSITE-ProRule annotation
Disulfide bondi519 ↔ 535PROSITE-ProRule annotation
Glycosylationi614 – 6141N-linked (GlcNAc...)Sequence Analysis
Glycosylationi699 – 6991N-linked (GlcNAc...)1 Publication
Glycosylationi729 – 7291N-linked (GlcNAc...)Sequence Analysis
Glycosylationi829 – 8291N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1009 – 10091N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1129 – 11291N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

The alpha- and beta-subunits are generated by a proteolytic cleavage by MBTPS1 protease at the Lys-928-Asp-929 bond.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ3T906.
PaxDbiQ3T906.
PRIDEiQ3T906.

PTM databases

PhosphoSiteiQ3T906.

Expressioni

Tissue specificityi

Expressed in the heart, whole brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.1 Publication

Gene expression databases

BgeeiQ3T906.
CleanExiHS_GNPTAB.
ExpressionAtlasiQ3T906. baseline and differential.
GenevisibleiQ3T906. HS.

Organism-specific databases

HPAiHPA042343.

Interactioni

Subunit structurei

Hexamer of two alpha, two beta and two gamma (GNPTG) subunits; disulfide-linked. The alpha and/or the beta subunits of the enzyme constitute the catalytic subunits.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
AENQ8WTP83EBI-1104907,EBI-8637627
FAM90A1Q86YD73EBI-1104907,EBI-6658203
PSMA1P257863EBI-1104907,EBI-359352
STAMBPL1Q96FJ03EBI-1104907,EBI-745021
ZNF250P15622-33EBI-1104907,EBI-10177272

Protein-protein interaction databases

BioGridi122576. 16 interactions.
IntActiQ3T906. 7 interactions.
STRINGi9606.ENSP00000299314.

Structurei

3D structure databases

ProteinModelPortaliQ3T906.
SMRiQ3T906. Positions 452-544.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati438 – 47336LNR 1Add
BLAST
Repeati505 – 54541LNR 2Add
BLAST
Domaini700 – 813114DMAP-interactionAdd
BLAST
Domaini1005 – 104036EF-handPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi465 – 49834Gly-richAdd
BLAST

Domaini

The DMAP-interaction domain mediates substrate recognition. It specifically recognizes a conformation-dependent protein determinant present in acid hydrolases (PubMed:23733939).1 Publication

Sequence similaritiesi

Belongs to the stealth family.Curated
Contains 1 DMAP-interaction domain.Curated
Contains 1 EF-hand domain.PROSITE-ProRule annotation
Contains 2 LNR (Lin/Notch) repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG05352.
GeneTreeiENSGT00390000006747.
HOVERGENiHBG057712.
InParanoidiQ3T906.
KOiK08239.
OMAiRKFVCLN.
OrthoDBiEOG75TMBF.
PhylomeDBiQ3T906.
TreeFamiTF324175.

Family and domain databases

InterProiIPR010506. DMAP1-bd.
IPR021520. DUF3184.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000800. Notch_dom.
[Graphical view]
PfamiPF06464. DMAP_binding. 1 hit.
PF11380. DUF3184. 1 hit.
PF00066. Notch. 2 hits.
[Graphical view]
SMARTiSM00004. NL. 2 hits.
[Graphical view]
SUPFAMiSSF90193. SSF90193. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS50258. LNR. 2 hits.
[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. AlignAdd to basket

Isoform 1 (identifier: Q3T906-1) [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
MLFKLLQRQT YTCLSHRYGL YVCFLGVVVT IVSAFQFGEV VLEWSRDQYH
60 70 80 90 100
VLFDSYRDNI AGKSFQNRLC LPMPIDVVYT WVNGTDLELL KELQQVREQM
110 120 130 140 150
EEEQKAMREI LGKNTTEPTK KSEKQLECLL THCIKVPMLV LDPALPANIT
160 170 180 190 200
LKDLPSLYPS FHSASDIFNV AKPKNPSTNV SVVVFDSTKD VEDAHSGLLK
210 220 230 240 250
GNSRQTVWRG YLTTDKEVPG LVLMQDLAFL SGFPPTFKET NQLKTKLPEN
260 270 280 290 300
LSSKVKLLQL YSEASVALLK LNNPKDFQEL NKQTKKNMTI DGKELTISPA
310 320 330 340 350
YLLWDLSAIS QSKQDEDISA SRFEDNEELR YSLRSIERHA PWVRNIFIVT
360 370 380 390 400
NGQIPSWLNL DNPRVTIVTH QDVFRNLSHL PTFSSPAIES HIHRIEGLSQ
410 420 430 440 450
KFIYLNDDVM FGKDVWPDDF YSHSKGQKVY LTWPVPNCAE GCPGSWIKDG
460 470 480 490 500
YCDKACNNSA CDWDGGDCSG NSGGSRYIAG GGGTGSIGVG QPWQFGGGIN
510 520 530 540 550
SVSYCNQGCA NSWLADKFCD QACNVLSCGF DAGDCGQDHF HELYKVILLP
560 570 580 590 600
NQTHYIIPKG ECLPYFSFAE VAKRGVEGAY SDNPIIRHAS IANKWKTIHL
610 620 630 640 650
IMHSGMNATT IHFNLTFQNT NDEEFKMQIT VEVDTREGPK LNSTAQKGYE
660 670 680 690 700
NLVSPITLLP EAEILFEDIP KEKRFPKFKR HDVNSTRRAQ EEVKIPLVNI
710 720 730 740 750
SLLPKDAQLS LNTLDLQLEH GDITLKGYNL SKSALLRSFL MNSQHAKIKN
760 770 780 790 800
QAIITDETND SLVAPQEKQV HKSILPNSLG VSERLQRLTF PAVSVKVNGH
810 820 830 840 850
DQGQNPPLDL ETTARFRVET HTQKTIGGNV TKEKPPSLIV PLESQMTKEK
860 870 880 890 900
KITGKEKENS RMEENAENHI GVTEVLLGRK LQHYTDSYLG FLPWEKKKYF
910 920 930 940 950
QDLLDEEESL KTQLAYFTDS KNTGRQLKDT FADSLRYVNK ILNSKFGFTS
960 970 980 990 1000
RKVPAHMPHM IDRIVMQELQ DMFPEEFDKT SFHKVRHSED MQFAFSYFYY
1010 1020 1030 1040 1050
LMSAVQPLNI SQVFDEVDTD QSGVLSDREI RTLATRIHEL PLSLQDLTGL
1060 1070 1080 1090 1100
EHMLINCSKM LPADITQLNN IPPTQESYYD PNLPPVTKSL VTNCKPVTDK
1110 1120 1130 1140 1150
IHKAYKDKNK YRFEIMGEEE IAFKMIRTNV SHVVGQLDDI RKNPRKFVCL
1160 1170 1180 1190 1200
NDNIDHNHKD AQTVKAVLRD FYESMFPIPS QFELPREYRN RFLHMHELQE
1210 1220 1230 1240 1250
WRAYRDKLKF WTHCVLATLI MFTIFSFFAE QLIALKRKIF PRRRIHKEAS

PNRIRV
Length:1,256
Mass (Da):143,622
Last modified:October 11, 2005 - v1
Checksum:i8B861154C516943E
GO
Isoform 2 (identifier: Q3T906-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     471-490: NSGGSRYIAGGGGTGSIGVG → KDVLNCNSFIFMEYFLLNHY
     491-1256: Missing.

Show »
Length:490
Mass (Da):55,983
Checksum:i9223139711337ED0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti392 – 3921I → V in AAV98624 (PubMed:16120602).Curated
Sequence conflicti901 – 9011Q → L in AAV98624 (PubMed:16120602).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti4 – 41K → Q in MLIIIA; also found in patients with intermediate phenotype between MLII and MLIIIA; no effect on protein abundance; decreased retention in the Golgi; mistargeted to lysosomes and plasma membrane; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 6 Publications
Corresponds to variant rs34159654 [ dbSNP | Ensembl ].
VAR_027509
Natural varianti15 – 151S → Y in MLIIIA; unknown pathological significance; no effect on protein abundance; decreased protein cleavage into alpha and beta subunits; decreased retention in the Golgi; mistargeted to lysosomes and plasma membrane; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 3 Publications
VAR_073124
Natural varianti81 – 811W → L in MLII; no effect on protein abundance; decreased localization to the Golgi; defects in protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 3 Publications
VAR_070831
Natural varianti182 – 1821V → D in MLII; unknown pathological significance; decreased localization to the Golgi; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_073125
Natural varianti190 – 1901D → V in MLIIIA; also found in patients with intermediate phenotype between MLII and MLIIIA; unknown pathological significance; no effect on protein abundance; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 1 Publication
Corresponds to variant rs34946266 [ dbSNP | Ensembl ].
VAR_053545
Natural varianti205 – 2051Q → P in MLII; unknown pathological significance. 1 Publication
VAR_073126
Natural varianti334 – 3341R → L in MLII; no effect on protein abundance; loss of localization to the Golgi; loss of protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_073127
Natural varianti334 – 3341R → Q in MLIIIA; no effect on protein abundance; loss of localization to the Golgi; loss of protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_073128
Natural varianti348 – 3481I → L in MLII; unknown pathological significance; no effect on protein abundance; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
Corresponds to variant rs7958709 [ dbSNP | Ensembl ].
VAR_027510
Natural varianti374 – 3741F → L in MLII and MLIIIA; no effect on protein abundance; no effect on localization to the Golgi; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_062807
Natural varianti399 – 3991S → F in MLIIIA; no effect on protein abundance; loss of localization to the Golgi; defects in protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 5 Publications
VAR_062808
Natural varianti403 – 4031I → T in MLIIIA; no effect on protein abundance; loss of localization to the Golgi; loss of protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 3 Publications
VAR_062809
Natural varianti407 – 4071D → A in MLIIIA; no effect on protein abundance; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_025416
Natural varianti442 – 4421C → Y in MLIIIA; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity toward some substrates. 2 Publications
VAR_062810
Natural varianti455 – 4551A → S Rare variant; found in individuals suffering from stuttering; unknown pathological significance. 1 Publication
VAR_073219
Natural varianti461 – 4611C → G in MLIIIA; no effect on protein abundance; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity toward some substrates. 2 Publications
VAR_062811
Natural varianti468 – 4681C → S in MLIIIA; patients with intermediate phenotype between MLII and MLIIIA; no effect on protein abundance; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity toward some substrates. 2 Publications
VAR_073129
Natural varianti505 – 5051C → Y in MLIIIA; unknown pathological significance; decreased localization to the Golgi; decreased protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 3 Publications
VAR_070832
Natural varianti523 – 5231C → R Found in a patient with mucolipidosis type II or III; unknown pathological significance; decreased localization to the Golgi; decreased protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_073130
Natural varianti587 – 5871R → P in MLIIIA; decreased localization to the Golgi; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_073131
Natural varianti592 – 5921A → T Found in a patient with mucolipidosis type II or III; unknown pathological significance; decreased localization to the Golgi; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_073132
Natural varianti625 – 6251F → L Rare variant; found in individuals suffering from stuttering; unknown pathological significance. 1 Publication
VAR_073220
Natural varianti662 – 6621A → G.1 Publication
VAR_025417
Natural varianti732 – 7321K → N in MLII; no effect on localization to the Golgi; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity toward some substrates. 3 Publications
VAR_070833
Natural varianti785 – 7851L → W Found in a patient with mucolipidosis type II or III; unknown pathological significance; no effect on localization to the Golgi; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity toward some substrates. 2 Publications
VAR_073133
Natural varianti926 – 9261Q → P in MLIIIA; no effect on localization to the Golgi; loss of protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_062812
Natural varianti928 – 9281K → R in MLII; unknown pathological significance. 1 Publication
VAR_073134
Natural varianti955 – 9551A → V in MLII; unknown pathological significance; no effect on protein abundance; no effect on localization to the Golgi; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_073135
Natural varianti956 – 9561H → R in MLIIIA; unknown pathological significance. 1 Publication
VAR_073136
Natural varianti956 – 9561H → Y in MLIIIA; no effect on protein abundance; no effect on localization to the Golgi. 2 Publications
VAR_062813
Natural varianti986 – 9861R → C in MLII; decreased protein abundance; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 4 Publications
VAR_070834
Natural varianti1001 – 10011L → P in MLII; no effect on protein abundance; decreased localization to the Golgi; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_062814
Natural varianti1018 – 10181D → G in MLIIIA; patients with intermediate phenotype between MLII and MLIIIA; unknown pathological significance; no effect on protein abundance; decreased localization to the Golgi; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_073137
Natural varianti1054 – 10541L → V in MLII; unknown pathological significance; no effect on localization to the Golgi; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_073138
Natural varianti1153 – 11531N → S in MLIIIA; no effect on protein abundance; no effect on localization to the Golgi; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 2 Publications
VAR_062815
Natural varianti1200 – 12001E → K Rare variant; found in individuals suffering from stuttering; unknown pathological significance. 1 Publication
VAR_073221
Natural varianti1236 – 12361K → M in MLII; decreased protein abundance; no effect on localization to the Golgi; does not suppress protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity. 3 Publications
VAR_027511

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei471 – 49020NSGGS…SIGVG → KDVLNCNSFIFMEYFLLNHY in isoform 2. 1 PublicationVSP_017338Add
BLAST
Alternative sequencei491 – 1256766Missing in isoform 2. 1 PublicationVSP_017339Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM085438 mRNA. Translation: CAJ30014.1.
AY687932 mRNA. Translation: AAV98624.1.
BC071687 mRNA. Translation: AAH71687.1.
BC042615 mRNA. Translation: AAH42615.1.
BC131787 mRNA. Translation: AAI31788.1.
AK056137 mRNA. Translation: BAB71102.1.
AB033034 mRNA. Translation: BAA86522.2.
CCDSiCCDS9088.1. [Q3T906-1]
RefSeqiNP_077288.2. NM_024312.4. [Q3T906-1]
UniGeneiHs.46850.

Genome annotation databases

EnsembliENST00000299314; ENSP00000299314; ENSG00000111670.
ENST00000549940; ENSP00000449150; ENSG00000111670. [Q3T906-2]
GeneIDi79158.
KEGGihsa:79158.
UCSCiuc001tit.3. human. [Q3T906-1]
uc001tiu.2. human. [Q3T906-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM085438 mRNA. Translation: CAJ30014.1.
AY687932 mRNA. Translation: AAV98624.1.
BC071687 mRNA. Translation: AAH71687.1.
BC042615 mRNA. Translation: AAH42615.1.
BC131787 mRNA. Translation: AAI31788.1.
AK056137 mRNA. Translation: BAB71102.1.
AB033034 mRNA. Translation: BAA86522.2.
CCDSiCCDS9088.1. [Q3T906-1]
RefSeqiNP_077288.2. NM_024312.4. [Q3T906-1]
UniGeneiHs.46850.

3D structure databases

ProteinModelPortaliQ3T906.
SMRiQ3T906. Positions 452-544.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122576. 16 interactions.
IntActiQ3T906. 7 interactions.
STRINGi9606.ENSP00000299314.

PTM databases

PhosphoSiteiQ3T906.

Polymorphism and mutation databases

BioMutaiGNPTAB.
DMDMi90185244.

Proteomic databases

MaxQBiQ3T906.
PaxDbiQ3T906.
PRIDEiQ3T906.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000299314; ENSP00000299314; ENSG00000111670.
ENST00000549940; ENSP00000449150; ENSG00000111670. [Q3T906-2]
GeneIDi79158.
KEGGihsa:79158.
UCSCiuc001tit.3. human. [Q3T906-1]
uc001tiu.2. human. [Q3T906-2]

Organism-specific databases

CTDi79158.
GeneCardsiGC12M102139.
GeneReviewsiGNPTAB.
HGNCiHGNC:29670. GNPTAB.
HPAiHPA042343.
MIMi252500. phenotype.
252600. phenotype.
607840. gene.
neXtProtiNX_Q3T906.
Orphaneti576. Mucolipidosis type 2.
577. Mucolipidosis type 3.
PharmGKBiPA128394710.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG05352.
GeneTreeiENSGT00390000006747.
HOVERGENiHBG057712.
InParanoidiQ3T906.
KOiK08239.
OMAiRKFVCLN.
OrthoDBiEOG75TMBF.
PhylomeDBiQ3T906.
TreeFamiTF324175.

Enzyme and pathway databases

BRENDAi2.7.8.17. 2681.

Miscellaneous databases

ChiTaRSiGNPTAB. human.
GenomeRNAii79158.
NextBioi68091.
PROiQ3T906.
SOURCEiSearch...

Gene expression databases

BgeeiQ3T906.
CleanExiHS_GNPTAB.
ExpressionAtlasiQ3T906. baseline and differential.
GenevisibleiQ3T906. HS.

Family and domain databases

InterProiIPR010506. DMAP1-bd.
IPR021520. DUF3184.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000800. Notch_dom.
[Graphical view]
PfamiPF06464. DMAP_binding. 1 hit.
PF11380. DUF3184. 1 hit.
PF00066. Notch. 2 hits.
[Graphical view]
SMARTiSM00004. NL. 2 hits.
[Graphical view]
SUPFAMiSSF90193. SSF90193. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS50258. LNR. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mucolipidosis II is caused by mutations in GNPTA encoding the alpha/beta GlcNAc-1-phosphotransferase."
    Tiede S., Storch S., Luebke T., Henrissat B., Bargal R., Raas-Rothschild A., Braulke T.
    Nat. Med. 11:1109-1112(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INVOLVEMENT IN MLII.
  2. "The alpha- and beta-subunits of the human UDP-N-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase are encoded by a single cDNA."
    Kudo M., Bao M., D'Souza A., Ying F., Pan H., Roe B.A., Canfield W.M.
    J. Biol. Chem. 280:36141-36149(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  3. Erratum
    Kudo M., Bao M., D'Souza A., Ying F., Pan H., Roe B.A., Canfield W.M.
    J. Biol. Chem. 280:42476-42476(2005)
  4. "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] (ISOFORMS 1 AND 2).
    Tissue: Liver.
  5. "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] OF 1-847 (ISOFORM 1).
  6. "Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
    DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 307-1256 (ISOFORM 1).
    Tissue: Brain.
  7. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  8. "Stealth proteins: in silico identification of a novel protein family rendering bacterial pathogens invisible to host immune defense."
    Sperisen P., Schmid C.D., Bucher P., Zilian O.
    PLoS Comput. Biol. 1:492-499(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS A STEALTH PROTEIN, PUTATIVE FUNCTION.
  9. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-699.
    Tissue: Liver.
  10. "Functions of the alpha, beta, and gamma subunits of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase."
    Qian Y., Lee I., Lee W.S., Qian M., Kudo M., Canfield W.M., Lobel P., Kornfeld S.
    J. Biol. Chem. 285:3360-3370(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
  11. "A key enzyme in the biogenesis of lysosomes is a protease that regulates cholesterol metabolism."
    Marschner K., Kollmann K., Schweizer M., Braulke T., Pohl S.
    Science 333:87-90(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION, GLYCOSYLATION, MUTAGENESIS OF ARG-925; LEU-927 AND LYS-928.
  12. "Two homozygous nonsense mutations of GNPTAB gene in two Chinese families with mucolipidosis II alpha/beta using targeted next-generation sequencing."
    Yang Y., Wu J., Liu H., Chen X., Wang Y., Zhao M., He X.
    Genomics 102:169-173(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MLII.
  13. "Mislocalization of phosphotransferase as a cause of mucolipidosis III alphabeta."
    van Meel E., Qian Y., Kornfeld S.A.
    Proc. Natl. Acad. Sci. U.S.A. 111:3532-3537(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS MLIIIA GLN-4 AND TYR-15.
  14. "Analysis of mucolipidosis II/III GNPTAB missense mutations identifies domains of UDP-GlcNAc:lysosomal enzyme GlcNAc-1-phosphotransferase involved in catalytic function and lysosomal enzyme recognition."
    Qian Y., van Meel E., Flanagan-Steet H., Yox A., Steet R., Kornfeld S.
    J. Biol. Chem. 290:3045-3056(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS MLII LEU-81; ASP-182; PRO-205; LEU-334; LEU-348; LEU-374; ASN-732; ARG-928; VAL-955; CYS-986; PRO-1001; VAL-1054 AND MET-1236, CHARACTERIZATION OF VARIANTS MLIIIA GLN-4; TYR-15; VAL-190; GLN-334; PHE-399; THR-403; ALA-407; TYR-442; GLY-461; SER-468; TYR-505; PRO-587; PRO-926; TYR-956; GLY-1018 AND SER-1153, CHARACTERIZATION OF VARIANTS ARG-523; THR-592 AND TRP-785.
  15. "Missense mutations in N-acetylglucosamine-1-phosphotransferase alpha/beta subunit gene in a patient with mucolipidosis III and a mild clinical phenotype."
    Tiede S., Muschol N., Reutter G., Cantz M., Ullrich K., Braulke T.
    Am. J. Med. Genet. A 137:235-240(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MLIIIA ALA-407, VARIANT GLY-662.
  16. "Mucolipidosis II (I-cell disease) and mucolipidosis IIIA (classical pseudo-Hurler polydystrophy) are caused by mutations in the GlcNAc-phosphotransferase alpha/beta-subunits precursor gene."
    Kudo M., Brem M.S., Canfield W.M.
    Am. J. Hum. Genet. 78:451-463(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MLIIIA GLN-4.
  17. "Missense mutation in the N-acetylglucosamine-1-phosphotransferase gene (GNPTA) in a patient with mucolipidosis II induces changes in the size and cellular distribution of GNPTG."
    Tiede S., Cantz M., Spranger J., Braulke T.
    Hum. Mutat. 27:830-831(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MLII MET-1236.
  18. Cited for: VARIANT MLIIIA PHE-399.
  19. "DNA-based diagnosis of mucolipidosis type IIIA and mucopolysacchariodisis type VI in a Chinese family: a chance of 1 in 7.6 trillion."
    Lam C.W., Yan M.S., Li C.K., Lau K.C., Tong S.F., Tang H.Y.
    Clin. Chim. Acta 376:250-252(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MLIIIA PRO-587.
  20. "Molecular analysis of cell lines from patients with mucolipidosis II and mucolipidosis III."
    Zarghooni M., Dittakavi S.S.
    Am. J. Med. Genet. A 149A:2753-2761(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MLII ASP-182; PRO-205; ASN-732; ARG-928; VAL-955 AND VAL-1054, VARIANT MLIIIA GLN-4, CHARACTERIZATION OF VARIANT MLIIIA GLN-4.
  21. "Molecular characterization of 22 novel UDP-N-acetylglucosamine-1-phosphate transferase alpha- and beta-subunit (GNPTAB) gene mutations causing mucolipidosis types IIalpha/beta and IIIalpha/beta in 46 patients."
    Tappino B., Chuzhanova N.A., Regis S., Dardis A., Corsolini F., Stroppiano M., Tonoli E., Beccari T., Rosano C., Mucha J., Blanco M., Szlago M., Di Rocco M., Cooper D.N., Filocamo M.
    Hum. Mutat. 30:E956-E973(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MLIIIA THR-403; TYR-442; GLY-461 AND PRO-926, VARIANT MLII PRO-1001.
  22. "Mucolipidosis II and III alpha/beta: mutation analysis of 40 Japanese patients showed genotype-phenotype correlation."
    Otomo T., Muramatsu T., Yorifuji T., Okuyama T., Nakabayashi H., Fukao T., Ohura T., Yoshino M., Tanaka A., Okamoto N., Inui K., Ozono K., Sakai N.
    J. Hum. Genet. 54:145-151(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MLII LEU-334 AND LEU-374, VARIANTS MLIIIA LEU-374; TYR-956 AND SER-1153.
  23. "Phenotype and genotype in mucolipidoses II and III alpha/beta: a study of 61 probands."
    Cathey S.S., Leroy J.G., Wood T., Eaves K., Simensen R.J., Kudo M., Stevenson R.E., Friez M.J.
    J. Med. Genet. 47:38-48(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MLIIIA GLN-4; TYR-15; VAL-190; GLN-334; PHE-399; SER-468; TYR-505; ARG-956 AND GLY-1018, VARIANT MLII LEU-348.
  24. "Mutations in the lysosomal enzyme-targeting pathway and persistent stuttering."
    Kang C., Riazuddin S., Mundorff J., Krasnewich D., Friedman P., Mullikin J.C., Drayna D.
    N. Engl. J. Med. 362:677-685(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS SER-455; LEU-625 AND LYS-1200, POSSIBLE INVOLVEMENT IN PERSISTENT STUTTERING.
  25. "Mucolipidosis type II alpha/beta with a homozygous missense mutation in the GNPTAB gene."
    Coutinho M.F., Santos L.S., Girisha K.M., Satyamoorthy K., Lacerda L., Prata M.J., Alves S.
    Am. J. Med. Genet. A 158A:1225-1228(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MLII CYS-986.
  26. "A novel intermediate mucolipidosis II/IIIalphabeta caused by GNPTAB mutation in the cytosolic N-terminal domain."
    Leroy J.G., Sillence D., Wood T., Barnes J., Lebel R.R., Friez M.J., Stevenson R.E., Steet R., Cathey S.S.
    Eur. J. Hum. Genet. 22:594-601(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MLIIIA GLN-4, CHARACTERIZATION OF VARIANT MLIIIA GLN-4.
  27. Cited for: VARIANT MLII LEU-81, VARIANTS MLIIIA PHE-399; THR-403 AND TYR-505.
  28. "Mucolipidosis II-related mutations inhibit the exit from the endoplasmic reticulum and proteolytic cleavage of GlcNAc-1-phosphotransferase precursor protein (GNPTAB)."
    De Pace R., Coutinho M.F., Koch-Nolte F., Haag F., Prata M.J., Alves S., Braulke T., Pohl S.
    Hum. Mutat. 35:368-376(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MLII LEU-81; CYS-986 AND MET-1236, VARIANT MLIIIA PHE-399, CHARACTERIZATION OF VARIANTS MLII LEU-81; CYS-986 AND MET-1236, CHARACTERIZATION OF VARIANT MLIIIA PHE-399, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, GLYCOSYLATION.
  29. "The DMAP interaction domain of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase is a substrate recognition module."
    Qian Y., Flanagan-Steet H., van Meel E., Steet R., Kornfeld S.A.
    Proc. Natl. Acad. Sci. U.S.A. 110:10246-10251(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MLII ASN-732, CHARACTERIZATION OF VARIANT MLII ASN-732, FUNCTION, SUBCELLULAR LOCATION.
  30. "Assessment of a targeted resequencing assay as a support tool in the diagnosis of lysosomal storage disorders."
    Fernandez-Marmiesse A., Morey M., Pineda M., Eiris J., Couce M.L., Castro-Gago M., Fraga J.M., Lacerda L., Gouveia S., Perez-Poyato M.S., Armstrong J., Castineiras D., Cocho J.A.
    Orphanet J. Rare Dis. 9:59-59(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS THR-592 AND TRP-785.
  31. "Dried blood spots allow targeted screening to diagnose mucopolysaccharidosis and mucolipidosis."
    Cobos P.N., Steglich C., Santer R., Lukacs Z., Gal A.
    JIMD Rep. 15:123-132(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MLII CYS-986, VARIANT ARG-523.

Entry informationi

Entry nameiGNPTA_HUMAN
AccessioniPrimary (citable) accession number: Q3T906
Secondary accession number(s): A2RRQ9
, Q3ZQK2, Q6IPW5, Q86TQ2, Q96N13, Q9ULL2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: October 11, 2005
Last modified: July 22, 2015
This is version 98 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

Miscellaneous

Due to the low pH in the endosomal/prelysosomal compartment, the lysosomal enzyme-MPR complex dissociates and then the enzyme is delivered to the lysosome. Between 5% and 20% of newly synthesized lysosomal enzymes escape the binding to the MPR in the Golgi apparatus and are secreted.
Stealth proteins are part of a protein family that is conserved from bacteria to higher eukaryotes. Family members were first identified in microbes as proteins that help pathogens to elude the host innate immune system. Microbial stealth proteins are most likely involved in the biosynthesis of exopolysaccharides. Stealth proteins are predicted to function as hexose-1-phosphoryltransferases.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.