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Q3T906 (GNPTA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-acetylglucosamine-1-phosphotransferase subunits alpha/beta

EC=2.7.8.17
Alternative name(s):
GlcNAc-1-phosphotransferase subunits alpha/beta
Stealth protein GNPTAB
UDP-N-acetylglucosamine-1-phosphotransferase subunits alpha/beta
Gene names
Name:GNPTAB
Synonyms:GNPTA, KIAA1208
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1256 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.10 Ref.23

Catalytic activity

UDP-N-acetyl-D-glucosamine + lysosomal-enzyme D-mannose = UMP + lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose. Ref.10

Subunit structure

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. Ref.10

Subcellular location

N-acetylglucosamine-1-phosphotransferase subunit alpha: Golgi apparatus membrane; Single-pass type I membrane protein Ref.1 Ref.2 Ref.11 Ref.22 Ref.23.

N-acetylglucosamine-1-phosphotransferase subunit beta: Golgi apparatus membrane; Single-pass type II membrane protein.

Tissue specificity

Expressed in the heart, whole brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Ref.2

Domain

The DMAP-interaction domain mediates substrate recognition. It specifically recognizes a conformation-dependent protein determinant present in acid hydrolases (Ref.23).

Post-translational modification

The alpha- and beta-subunits are generated by a proteolytic cleavage by MBTPS1 protease at the Lys-928-Asp-929 bond (Ref.11).

Involvement in disease

Mucolipidosis type II (MLII) [MIM:252500]: Fatal, 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23

Mucolipidosis type III complementation group A (MLIIIA) [MIM:252600]: Autosomal 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22

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.

Sequence similarities

Belongs to the stealth family.

Contains 1 DMAP-interaction domain.

Contains 1 EF-hand domain.

Contains 2 LNR (Lin/Notch) repeats.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q3T906-1)

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.
Isoform 2 (identifier: Q3T906-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 928928N-acetylglucosamine-1-phosphotransferase subunit alpha
PRO_0000225008
Chain929 – 1256328N-acetylglucosamine-1-phosphotransferase subunit beta
PRO_0000225009

Regions

Transmembrane22 – 4221Helical; Potential
Transmembrane1215 – 123521Helical; Potential
Repeat438 – 47336LNR 1
Repeat505 – 54541LNR 2
Domain700 – 813114DMAP-interaction
Domain1005 – 104036EF-hand
Calcium binding1018 – 102912 Potential
Compositional bias465 – 49834Gly-rich

Sites

Metal binding4491Calcium By similarity
Metal binding4641Calcium By similarity
Metal binding4671Calcium By similarity
Metal binding5161Calcium By similarity
Metal binding5311Calcium By similarity
Metal binding5341Calcium By similarity
Site928 – 9292Cleavage; by MBTPS1

Amino acid modifications

Glycosylation831N-linked (GlcNAc...) Potential
Glycosylation1141N-linked (GlcNAc...) Potential
Glycosylation1481N-linked (GlcNAc...) Potential
Glycosylation1791N-linked (GlcNAc...) Potential
Glycosylation2501N-linked (GlcNAc...) Potential
Glycosylation6141N-linked (GlcNAc...) Potential
Glycosylation6991N-linked (GlcNAc...) Ref.9
Glycosylation7291N-linked (GlcNAc...) Potential
Glycosylation8291N-linked (GlcNAc...) Potential
Glycosylation10091N-linked (GlcNAc...) Potential
Glycosylation11291N-linked (GlcNAc...) Potential
Disulfide bond438 ↔ 461 By similarity
Disulfide bond452 ↔ 468 By similarity
Disulfide bond505 ↔ 528 By similarity
Disulfide bond519 ↔ 535 By similarity

Natural variations

Alternative sequence471 – 49020NSGGS…SIGVG → KDVLNCNSFIFMEYFLLNHY in isoform 2.
VSP_017338
Alternative sequence491 – 1256766Missing in isoform 2.
VSP_017339
Natural variant41K → Q in MLIIIA; in MLII; intermediate phenotype between MLII and MLIIIA; shows a distinct, consistent phenotype similar to MLII in physical and radiographic features and to MLIIIA in psychomotor development and life expectancy. Ref.14 Ref.20
Corresponds to variant rs34159654 [ dbSNP | Ensembl ].
VAR_027509
Natural variant811W → L in MLII; defects in protein cleavage into alpha and beta subunits; impaired subcellular location. Ref.21 Ref.22
VAR_070831
Natural variant1901D → V.
Corresponds to variant rs34946266 [ dbSNP | Ensembl ].
VAR_053545
Natural variant3481I → L.
Corresponds to variant rs7958709 [ dbSNP | Ensembl ].
VAR_027510
Natural variant3741F → L in MLIIIA; also in MLII. Ref.18
VAR_062807
Natural variant3991S → F in MLIIIA; defects in protein cleavage into alpha and beta subunits; impaired subcellular location. Ref.16 Ref.21 Ref.22
VAR_062808
Natural variant4031I → T in MLIIIA. Ref.17 Ref.21
VAR_062809
Natural variant4071D → A in MLIIIA. Ref.13
VAR_025416
Natural variant4421C → Y in MLIIIA. Ref.17
VAR_062810
Natural variant4611C → G in MLIIIA. Ref.17
VAR_062811
Natural variant5051C → Y in MLIIIA; unknown pathological significance; heterozygous. Ref.21
VAR_070832
Natural variant6621A → G. Ref.13
VAR_025417
Natural variant7321K → N in MLII; impaired substrate recognition. Ref.23
VAR_070833
Natural variant9261Q → P in MLIIIA. Ref.17
VAR_062812
Natural variant9561H → Y in MLIIIA. Ref.18
VAR_062813
Natural variant9861R → C in MLII; does not suppress protein cleavage into alpha and beta subunits; does not affect subcellular location. Ref.19 Ref.22
VAR_070834
Natural variant10011L → P in MLII. Ref.17
VAR_062814
Natural variant11531N → S in MLIIIA. Ref.18
VAR_062815
Natural variant12361K → M in MLII; does not suppress protein cleavage into alpha and beta subunits; does not affect subcellular location; decreased mRNA stability. Ref.15 Ref.22
VAR_027511

Experimental info

Mutagenesis9251R → A: Abolishes proteolytic cleavage by MBTPS1. Ref.11
Mutagenesis9271L → A: Abolishes proteolytic cleavage by MBTPS1. Ref.11
Mutagenesis9281K → A: Abolishes proteolytic cleavage by MBTPS1. Ref.11
Sequence conflict3921I → V in AAV98624. Ref.2
Sequence conflict9011Q → L in AAV98624. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 8B861154C516943E

FASTA1,256143,622
        10         20         30         40         50         60 
MLFKLLQRQT YTCLSHRYGL YVCFLGVVVT IVSAFQFGEV VLEWSRDQYH VLFDSYRDNI 

        70         80         90        100        110        120 
AGKSFQNRLC LPMPIDVVYT WVNGTDLELL KELQQVREQM EEEQKAMREI LGKNTTEPTK 

       130        140        150        160        170        180 
KSEKQLECLL THCIKVPMLV LDPALPANIT LKDLPSLYPS FHSASDIFNV AKPKNPSTNV 

       190        200        210        220        230        240 
SVVVFDSTKD VEDAHSGLLK GNSRQTVWRG YLTTDKEVPG LVLMQDLAFL SGFPPTFKET 

       250        260        270        280        290        300 
NQLKTKLPEN LSSKVKLLQL YSEASVALLK LNNPKDFQEL NKQTKKNMTI DGKELTISPA 

       310        320        330        340        350        360 
YLLWDLSAIS QSKQDEDISA SRFEDNEELR YSLRSIERHA PWVRNIFIVT NGQIPSWLNL 

       370        380        390        400        410        420 
DNPRVTIVTH QDVFRNLSHL PTFSSPAIES HIHRIEGLSQ KFIYLNDDVM FGKDVWPDDF 

       430        440        450        460        470        480 
YSHSKGQKVY LTWPVPNCAE GCPGSWIKDG YCDKACNNSA CDWDGGDCSG NSGGSRYIAG 

       490        500        510        520        530        540 
GGGTGSIGVG QPWQFGGGIN SVSYCNQGCA NSWLADKFCD QACNVLSCGF DAGDCGQDHF 

       550        560        570        580        590        600 
HELYKVILLP NQTHYIIPKG ECLPYFSFAE VAKRGVEGAY SDNPIIRHAS IANKWKTIHL 

       610        620        630        640        650        660 
IMHSGMNATT IHFNLTFQNT NDEEFKMQIT VEVDTREGPK LNSTAQKGYE NLVSPITLLP 

       670        680        690        700        710        720 
EAEILFEDIP KEKRFPKFKR HDVNSTRRAQ EEVKIPLVNI SLLPKDAQLS LNTLDLQLEH 

       730        740        750        760        770        780 
GDITLKGYNL SKSALLRSFL MNSQHAKIKN QAIITDETND SLVAPQEKQV HKSILPNSLG 

       790        800        810        820        830        840 
VSERLQRLTF PAVSVKVNGH DQGQNPPLDL ETTARFRVET HTQKTIGGNV TKEKPPSLIV 

       850        860        870        880        890        900 
PLESQMTKEK KITGKEKENS RMEENAENHI GVTEVLLGRK LQHYTDSYLG FLPWEKKKYF 

       910        920        930        940        950        960 
QDLLDEEESL KTQLAYFTDS KNTGRQLKDT FADSLRYVNK ILNSKFGFTS RKVPAHMPHM 

       970        980        990       1000       1010       1020 
IDRIVMQELQ DMFPEEFDKT SFHKVRHSED MQFAFSYFYY LMSAVQPLNI SQVFDEVDTD 

      1030       1040       1050       1060       1070       1080 
QSGVLSDREI RTLATRIHEL PLSLQDLTGL EHMLINCSKM LPADITQLNN IPPTQESYYD 

      1090       1100       1110       1120       1130       1140 
PNLPPVTKSL VTNCKPVTDK IHKAYKDKNK YRFEIMGEEE IAFKMIRTNV SHVVGQLDDI 

      1150       1160       1170       1180       1190       1200 
RKNPRKFVCL NDNIDHNHKD AQTVKAVLRD FYESMFPIPS QFELPREYRN RFLHMHELQE 

      1210       1220       1230       1240       1250 
WRAYRDKLKF WTHCVLATLI MFTIFSFFAE QLIALKRKIF PRRRIHKEAS PNRIRV 

« Hide

Isoform 2 [UniParc].

Checksum: 9223139711337ED0
Show »

FASTA49055,983

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"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.
[14]"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.
[15]"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.
[16]"When Mucolipidosis III meets Mucolipidosis II: GNPTA gene mutations in 24 patients."
Bargal R., Zeigler M., Abu-Libdeh B., Zuri V., Mandel H., Ben Neriah Z., Stewart F., Elcioglu N., Hindi T., Le Merrer M., Bach G., Raas-Rothschild A.
Mol. Genet. Metab. 88:359-363(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MLIIIA PHE-399.
[17]"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.
[18]"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 MLIIIA LEU-374; TYR-956 AND SER-1153.
[19]"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.
[20]"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. 0:0-0(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MLIIIA GLN-4, CHARACTERIZATION OF VARIANT MLIIIA GLN-4.
[21]"Mucolipidosis II and III alpha/beta in Brazil: analysis of the GNPTAB gene."
Cury G.K., Matte U., Artigalas O., Alegra T., Velho R.V., Sperb F., Burin M.G., Ribeiro E.M., Lourenco C.M., Kim C.A., Valadares E.R., Galera M.F., Acosta A.X., Schwartz I.V.
Gene 524:59-64(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MLII LEU-81, VARIANTS MLIIIA PHE-399; THR-403 AND TYR-505.
[22]"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. 0:0-0(2013) [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.
[23]"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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_077288.2. NM_024312.4.
UniGeneHs.46850.

3D structure databases

ProteinModelPortalQ3T906.
SMRQ3T906. Positions 448-544.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122576. 5 interactions.
IntActQ3T906. 2 interactions.
STRING9606.ENSP00000299314.

PTM databases

PhosphoSiteQ3T906.

Polymorphism databases

DMDM90185244.

Proteomic databases

PaxDbQ3T906.
PRIDEQ3T906.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000299314; ENSP00000299314; ENSG00000111670. [Q3T906-1]
ENST00000549940; ENSP00000449150; ENSG00000111670. [Q3T906-2]
GeneID79158.
KEGGhsa:79158.
UCSCuc001tit.3. human. [Q3T906-1]
uc001tiu.2. human. [Q3T906-2]

Organism-specific databases

CTD79158.
GeneCardsGC12M102139.
HGNCHGNC:29670. GNPTAB.
HPAHPA042343.
MIM252500. phenotype.
252600. phenotype.
607840. gene.
neXtProtNX_Q3T906.
Orphanet576. Mucolipidosis type 2.
577. Mucolipidosis type 3.
PharmGKBPA128394710.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG05352.
HOVERGENHBG057712.
InParanoidQ3T906.
KOK08239.
OMAFYESMFP.
OrthoDBEOG75TMBF.
PhylomeDBQ3T906.
TreeFamTF324175.

Enzyme and pathway databases

BRENDA2.7.8.17. 2681.

Gene expression databases

ArrayExpressQ3T906.
BgeeQ3T906.
CleanExHS_GNPTAB.
GenevestigatorQ3T906.

Family and domain databases

InterProIPR010506. DMAP1-bd.
IPR021520. DUF3184.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000800. Notch_dom.
[Graphical view]
PfamPF06464. DMAP_binding. 1 hit.
PF11380. DUF3184. 1 hit.
PF00066. Notch. 2 hits.
[Graphical view]
SMARTSM00004. NL. 2 hits.
[Graphical view]
SUPFAMSSF90193. SSF90193. 1 hit.
PROSITEPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS50258. LNR. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGNPTAB. human.
GenomeRNAi79158.
NextBio68091.
PROQ3T906.
SOURCESearch...

Entry information

Entry nameGNPTA_HUMAN
AccessionPrimary (citable) accession number: Q3T906
Secondary accession number(s): A2RRQ9 expand/collapse secondary AC list , Q3ZQK2, Q6IPW5, Q86TQ2, Q96N13, Q9ULL2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: October 11, 2005
Last modified: April 16, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM