SULF2

From Wikipedia, the free encyclopedia

Sulfatase 2

Identifiers

SULF2; DKFZp313E091; FLJ90554; HSULF-2; KIAA1247; MGC126411

External IDs

OMIM: 610013 MGI: 1919293 HomoloGene: 10313

Gene ontology
Molecular Function:	• arylsulfatase activity • calcium ion binding • sulfuric ester hydrolase activity • hydrolase activity
Cellular Component:	• extracellular space • endoplasmic reticulum • cell surface
Biological Process:	• metabolic process • heparan sulfate proteoglycan metabolic process

Orthologs

Human

Mouse

Refseq

NM_018837 (mRNA)
NP_061325 (protein)

NM_028072 (mRNA)
NP_082348 (protein)

Location

Chr 20: 45.72 - 45.85 Mb

Chr 2: 165.77 - 165.85 Mb

Pubmed search

[1]

[2]

Sulfatase 2, also known as SULF2, is a human gene.^[1]

Heparan sulfate proteoglycans (HSPGs) act as coreceptors for numerous heparin-binding growth factors and cytokines and are involved in cell signaling. Heparan sulfate 6-O-endosulfatases, such as SULF2, selectively remove 6-O-sulfate groups from heparan sulfate. This activity modulates the effects of heparan sulfate by altering binding sites for signaling molecules (Dai et al., 2005).[supplied by OMIM]^[1]

[edit] References

^ ^a ^b Entrez Gene: SULF2 sulfatase 2.

[edit] Further reading

Nakajima D, Okazaki N, Yamakawa H, et al. (2003). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones.". DNA Res. 9 (3): 99-106. PMID 12168954.
Nagase T, Ishikawa K, Kikuno R, et al. (2000). "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.". DNA Res. 6 (5): 337-45. PMID 10574462.
Fossey SC, Mychaleckyj JC, Pendleton JK, et al. (2001). "A high-resolution 6.0-megabase transcript map of the type 2 diabetes susceptibility region on human chromosome 20.". Genomics 76 (1-3): 45-57. doi:10.1006/geno.2001.6584. PMID 11549316.
Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20.". Nature 414 (6866): 865-71. doi:10.1038/414865a. PMID 11780052.
Morimoto-Tomita M, Uchimura K, Werb Z, et al. (2003). "Cloning and characterization of two extracellular heparin-degrading endosulfatases in mice and humans.". J. Biol. Chem. 277 (51): 49175-85. doi:10.1074/jbc.M205131200. PMID 12368295.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932.
Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.". Genome Res. 13 (10): 2265-70. doi:10.1101/gr.1293003. PMID 12975309.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334.
Dai Y, Yang Y, MacLeod V, et al. (2006). "HSulf-1 and HSulf-2 are potent inhibitors of myeloma tumor growth in vivo.". J. Biol. Chem. 280 (48): 40066-73. doi:10.1074/jbc.M508136200. PMID 16192265.
Morimoto-Tomita M, Uchimura K, Bistrup A, et al. (2006). "Sulf-2, a proangiogenic heparan sulfate endosulfatase, is upregulated in breast cancer.". Neoplasia 7 (11): 1001-10. PMID 16331886.
Uchimura K, Morimoto-Tomita M, Bistrup A, et al. (2006). "HSulf-2, an extracellular endoglucosamine-6-sulfatase, selectively mobilizes heparin-bound growth factors and chemokines: effects on VEGF, FGF-1, and SDF-1.". BMC Biochem. 7: 2. doi:10.1186/1471-2091-7-2. PMID 16417632.