Exostosin-like 2
Details
- Name
- Exostosin-like 2
- Kind
- protein
- Synonyms
- 2.4.1.223
- Alpha-1,4-N-acetylhexosaminyltransferase EXTL2
- Alpha-GalNAcT EXTL2
- EXT-related protein 2
- EXTR2
- Glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase
- Gene Name
- EXTL2
- UniProtKB Entry
- Q9UBQ6Swiss-Prot
- Organism
- Humans
- NCBI Taxonomy ID
- 9606
- Amino acid sequence
>lcl|BSEQ0013226|Exostosin-like 2 MRCCHICKLPGRVMGIRVLRLSLVVILVLLLVAGALTALLPSVKEDKMLMLRREIKSQGK STMDSFTLIMQTYNRTDLLLKLLNHYQAVPNLHKVIVVWNNIGEKAPDELWNSLGPHPIP VIFKQQTANRMRNRLQVFPELETNAVLMVDDDTLISTPDLVFAFSVWQQFPDQIVGFVPR KHVSTSSGIYSYGSFEMQAPGSGNGDQYSMVLIGASFFNSKYLELFQRQPAAVHALIDDT QNCDDIAMNFIIAKHIGKTSGIFVKPVNMDNLEKETNSGYSGMWHRAEHALQRSYCINKL VNIYDSMPLRYSNIMISQFGFPYANYKRKI
- Number of residues
- 330
- Molecular Weight
- 37465.365
- Theoretical pI
- Not Available
- GO Classification
- Functionsglucuronylgalactosylproteoglycan 4-beta-N-acetylgalactosaminyltransferase activity / glycosaminoglycan binding / manganese ion bindingComponentscytosol / extracellular region / nucleoplasm
- General Function
- Glycosyltransferase required for the biosynthesis of heparan-sulfate and responsible for the alternating addition of beta-1-4-linked glucuronic acid (GlcA) and alpha-1-4-linked N-acetylglucosamine (GlcNAc) units to nascent heparan sulfate chains
- Specific Function
- alpha-1,4-N-acetylgalactosaminyltransferase activity
- Pfam Domain Function
- Glyco_transf_64 (PF09258)
- Signal Regions
- Not Available
- Transmembrane Regions
- 23-43
- Cellular Location
- Endoplasmic reticulum membrane
- Gene sequence
>lcl|BSEQ0013227|Exostosin-like 2 (EXTL2) ATGAGGTGTTGCCACATCTGCAAACTTCCTGGGAGAGTAATGGGGATTCGAGTGCTTCGA TTATCTTTGGTGGTCATCCTCGTATTATTACTGGTAGCTGGTGCTTTGACTGCCTTACTT CCCAGTGTTAAAGAAGACAAGATGCTCATGTTGCGTAGGGAAATAAAATCCCAGGGCAAG TCCACCATGGACTCCTTTACTCTCATAATGCAGACGTACAACAGAACAGATCTCTTATTG AAACTTTTAAATCATTATCAGGCTGTACCAAATCTGCACAAAGTGATTGTGGTATGGAAC AATATTGGAGAGAAGGCACCAGATGAATTATGGAATTCTCTAGGGCCCCACCCTATCCCT GTGATCTTCAAACAACAGACAGCAAACAGGATGAGAAATCGACTCCAGGTCTTTCCTGAA CTGGAAACCAATGCAGTGTTGATGGTAGATGATGACACACTCATCAGCACCCCAGACCTT GTTTTTGCTTTCTCAGTTTGGCAGCAATTTCCTGATCAAATTGTAGGATTTGTTCCTAGA AAGCACGTCTCTACTTCATCAGGTATCTACAGTTATGGAAGTTTTGAAATGCAAGCACCA GGGTCTGGAAATGGTGACCAGTACTCTATGGTGCTGATTGGAGCCTCATTCTTCAATAGC AAATATCTTGAATTATTTCAGAGGCAACCTGCAGCTGTCCATGCTTTGATAGATGATACT CAAAACTGTGATGATATTGCCATGAATTTTATCATTGCCAAGCATATTGGCAAGACTTCA GGGATATTTGTGAAGCCTGTAAACATGGACAATTTGGAAAAAGAAACCAACAGTGGCTAT TCTGGAATGTGGCATCGAGCTGAGCACGCTCTGCAGAGGTCTTATTGTATAAATAAGCTT GTTAATATCTATGATAGCATGCCCTTAAGATACTCCAACATTATGATTTCCCAGTTTGGT TTTCCATATGCCAACTACAAAAGAAAAATATAA
- Chromosome Location
- 1
- Locus
- 1p21.2
- External Identifiers
Resource Link UniProtKB ID Q9UBQ6 UniProtKB Entry Name EXTL2_HUMAN GeneCard ID EXTL2 HGNC ID HGNC:3516 KEGG ID hsa:2135 NCBI Gene ID 2135 - General References
- Wuyts W, Van Hul W, Hendrickx J, Speleman F, Wauters J, De Boulle K, Van Roy N, Van Agtmael T, Bossuyt P, Willems PJ: Identification and characterization of a novel member of the EXT gene family, EXTL2. Eur J Hum Genet. 1997 Nov-Dec;5(6):382-9. [Article]
- Saito T, Seki N, Yamauchi M, Tsuji S, Hayashi A, Kozuma S, Hori T: Structure, chromosomal location, and expression profile of EXTR1 and EXTR2, new members of the multiple exostoses gene family. Biochem Biophys Res Commun. 1998 Feb 4;243(1):61-6. [Article]
- McCormick C, Duncan G, Goutsos KT, Tufaro F: The putative tumor suppressors EXT1 and EXT2 form a stable complex that accumulates in the Golgi apparatus and catalyzes the synthesis of heparan sulfate. Proc Natl Acad Sci U S A. 2000 Jan 18;97(2):668-73. [Article]
- Kitagawa H, Shimakawa H, Sugahara K: The tumor suppressor EXT-like gene EXTL2 encodes an alpha1, 4-N-acetylhexosaminyltransferase that transfers N-acetylgalactosamine and N-acetylglucosamine to the common glycosaminoglycan-protein linkage region. The key enzyme for the chain initiation of heparan sulfate. J Biol Chem. 1999 May 14;274(20):13933-7. [Article]
- 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 TO, 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: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Uridine-Diphosphate-N-Acetylgalactosamine experimental unknown target Details Uridine-Diphosphate-N-Acetylglucosamine experimental unknown target Details Uridine-5'-Diphosphate experimental unknown target Details