Q3T906 (GNPTA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Cleaved into the following 2 chains:

1. N-acetylglucosamine-1-phosphotransferase subunit alpha
2. N-acetylglucosamine-1-phosphotransferase subunit beta

Gene names

Name:	GNPTAB
Synonyms:	GNPTA, KIAA1208

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1256 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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
Catalytic activity	UDP-N-acetyl-D-glucosamine + lysosomal-enzyme D-mannose = UMP + lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose.
Subunit structure	Hexamer of two alpha, two beta and two gamma subunits; disulfide-linked. It is believed that the alpha and/or the beta subunit of the enzyme contain the catalytic portion and that the gamma subunit functions in recognition of the lysosomal enzymes By similarity.
Subcellular location	N-acetylglucosamine-1-phosphotransferase subunit alpha: Golgi apparatus membrane; Single-pass type I membrane protein Ref.1 Ref.2. 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
Post-translational modification	The alpha- and beta-subunits appear to be generated by a proteolytic cleavage at the Lys-928-Asp-929 bond.
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.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 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.10 Ref.11 Ref.13 Ref.14 Ref.15
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 EF-hand domain. Contains 2 LNR (Lin/Notch) repeats.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Mucolipidosis
Domain	Repeat Signal-anchor Transmembrane Transmembrane helix
Ligand	Calcium Metal-binding
Molecular function	Transferase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate phosphorylation Inferred from electronic annotation. Source: Compara cell differentiation Inferred from electronic annotation. Source: InterPro protein secretion Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: InterPro
Molecular_function	UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity Inferred from electronic annotation. Source: EC calcium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 928	928	N-acetylglucosamine-1-phosphotransferase subunit alpha		PRO_0000225008
	Chain	929 – 1256	328	N-acetylglucosamine-1-phosphotransferase subunit beta		PRO_0000225009
Regions
	Transmembrane	22 – 42	21	Helical; Potential
	Transmembrane	1215 – 1235	21	Helical; Potential
	Repeat	438 – 473	36	LNR 1
	Repeat	505 – 545	41	LNR 2
	Domain	1005 – 1040	36	EF-hand
	Calcium binding	1018 – 1029	12	Potential
	Compositional bias	465 – 498	34	Gly-rich
Sites
	Metal binding	449	1	Calcium By similarity
	Metal binding	464	1	Calcium By similarity
	Metal binding	467	1	Calcium By similarity
	Metal binding	516	1	Calcium By similarity
	Metal binding	531	1	Calcium By similarity
	Metal binding	534	1	Calcium By similarity
Amino acid modifications
	Glycosylation	83	1	N-linked (GlcNAc...) Potential
	Glycosylation	114	1	N-linked (GlcNAc...) Potential
	Glycosylation	148	1	N-linked (GlcNAc...) Potential
	Glycosylation	179	1	N-linked (GlcNAc...) Potential
	Glycosylation	250	1	N-linked (GlcNAc...) Potential
	Glycosylation	614	1	N-linked (GlcNAc...) Potential
	Glycosylation	699	1	N-linked (GlcNAc...) Ref.9
	Glycosylation	729	1	N-linked (GlcNAc...) Potential
	Glycosylation	829	1	N-linked (GlcNAc...) Potential
	Glycosylation	1009	1	N-linked (GlcNAc...) Potential
	Glycosylation	1129	1	N-linked (GlcNAc...) Potential
	Disulfide bond	438 ↔ 461		By similarity
	Disulfide bond	452 ↔ 468		By similarity
	Disulfide bond	505 ↔ 528		By similarity
	Disulfide bond	519 ↔ 535		By similarity
Natural variations
	Alternative sequence	471 – 490	20	NSGGS…SIGVG → KDVLNCNSFIFMEYFLLNHY in isoform 2.		VSP_017338
	Alternative sequence	491 – 1256	766	Missing in isoform 2.		VSP_017339
	Natural variant	4	1	K → Q in MLIIIA. Ref.11 Corresponds to variant rs34159654 [ dbSNP | Ensembl ].		VAR_027509
	Natural variant	190	1	D → V. Corresponds to variant rs34946266 [ dbSNP | Ensembl ].		VAR_053545
	Natural variant	348	1	I → L. Corresponds to variant rs7958709 [ dbSNP | Ensembl ].		VAR_027510
	Natural variant	374	1	F → L in MLIIIA; also in MLII. Ref.15		VAR_062807
	Natural variant	399	1	S → F in MLIIIA. Ref.13		VAR_062808
	Natural variant	403	1	I → T in MLIIIA. Ref.14		VAR_062809
	Natural variant	407	1	D → A in MLIIIA. Ref.10		VAR_025416
	Natural variant	442	1	C → Y in MLIIIA. Ref.14		VAR_062810
	Natural variant	461	1	C → G in MLIIIA. Ref.14		VAR_062811
	Natural variant	662	1	A → G. Ref.10		VAR_025417
	Natural variant	926	1	Q → P in MLIIIA. Ref.14		VAR_062812
	Natural variant	956	1	H → Y in MLIIIA. Ref.15		VAR_062813
	Natural variant	1001	1	L → P in MLII. Ref.14		VAR_062814
	Natural variant	1153	1	N → S in MLIIIA. Ref.15		VAR_062815
	Natural variant	1236	1	K → M in MLII; not only impairs lysosomal enzyme targeting but also the availability of intact GNPTG required for phosphotransferase activity and assembly of subunits. Ref.12		VAR_027511
Experimental info
	Sequence conflict	392	1	I → V in AAV98624. Ref.2
	Sequence conflict	901	1	Q → L in AAV98624. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 11, 2005. Version 1. Checksum: 8B861154C516943E	FASTA	1,256	143,622
	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
	Isoform 2 [UniParc]. Checksum: 9223139711337ED0	FASTA	490	55,983
	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 KDVLNCNSFI 490 FMEYFLLNHY

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. Tissue: Liver.
[10]	"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.
[11]	"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.
[12]	"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, CHARACTERIZATION OF VARIANT MLII MET-1236.
[13]	"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.
[14]	"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.
[15]	"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.
+	Additional computationally mapped references.

Web resources

GeneReviews

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.
IPI	IPI00382432. IPI00735667.
RefSeq	NP_077288.2. NM_024312.4.
UniGene	Hs.46850.
3D structure databases
ProteinModelPortal	Q3T906.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q3T906. 2 interactions.
STRING	9606.ENSP00000299314.
PTM databases
PhosphoSite	Q3T906.
Polymorphism databases
DMDM	90185244.
Proteomic databases
PaxDb	Q3T906.
PRIDE	Q3T906.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000299314; ENSP00000299314; ENSG00000111670. ENST00000549940; ENSP00000449150; ENSG00000111670.
GeneID	79158.
KEGG	hsa:79158.
UCSC	uc001tit.3. human. uc001tiu.2. human.
Organism-specific databases
CTD	79158.
GeneCards	GC12M102139.
HGNC	HGNC:29670. GNPTAB.
HPA	HPA042343.
MIM	252500. phenotype. 252600. phenotype. 607840. gene.
neXtProt	NX_Q3T906.
Orphanet	576. Mucolipidosis type 2. 577. Mucolipidosis type 3.
PharmGKB	PA128394710.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG05352.
HOVERGEN	HBG057712.
InParanoid	Q3T906.
KO	K08239.
OMA	SQFELPR.
OrthoDB	EOG4TXBR2.
PhylomeDB	Q3T906.
Enzyme and pathway databases
BRENDA	2.7.8.17. 2681.
Gene expression databases
ArrayExpress	Q3T906.
Bgee	Q3T906.
CleanEx	HS_GNPTAB.
Genevestigator	Q3T906.
GermOnline	ENSG00000111670. Homo sapiens.
Family and domain databases
InterPro	IPR010506. DMAP1-bd. IPR021520. DUF3184. IPR018247. EF_Hand_1_Ca_BS. IPR002048. EF_hand_dom. IPR000800. Notch_dom. [Graphical view]
Pfam	PF06464. DMAP_binding. 1 hit. PF11380. DUF3184. 1 hit. PF00066. Notch. 2 hits. [Graphical view]
SMART	SM00004. NL. 2 hits. [Graphical view]
SUPFAM	SSF90193. Notch_region. 1 hit.
PROSITE	PS00018. EF_HAND_1. 1 hit. PS50222. EF_HAND_2. 1 hit. PS50258. LNR. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	GNPTAB. human.
GenomeRNAi	79158.
NextBio	68091.
SOURCE	Search...

Entry information

Entry name

GNPTA_HUMAN

Accession

Primary (citable) accession number: Q3T906
Secondary accession number(s): A2RRQ9 , Q3ZQK2, Q6IPW5, Q86TQ2, Q96N13, Q9ULL2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	October 11, 2005
Last modified:	May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.