SLC35B2

  • Official Full Name

    solute carrier family 35, member B2
  • Overview

    Sulfotransferases (e.g., SULT4A1; MIM 608359) use an activated form of sulfate, 3-prime-phosphoadenosine;5-prime-phosphosulfate (PAPS), as a common sulfate donor for sulfation of glycoproteins, proteoglycans, and;glycolipids in the endoplasmic reticulum and Golgi apparatus. SLC35B2 is located in the microsomal membrane and;transports PAPS from the cytosol, where it is synthesized, into the Golgi lumen (Kamiyama et al., 2003 (PubMed;12716889)).
  • Synonyms

    SLC35B2;solute carrier family 35, member B2;adenosine 3-phospho 5-phosphosulfate transporter 1;UGTrel4;PAPS transporter 1;putative MAPK-activating protein PM15;putative NF-kappa-B-activating protein 48;solute carrier family 35 member B2 variant 2
Cat.# Product name Source (Host) Species Tag Protein Length Price
SLC35B2-11667Z Recombinant Zebrafish SLC35B2 Mammalian Cells Zebrafish His
SLC35B2-606HCL Recombinant Human SLC35B2 lysate HEK293 Human Non
RFL22028DF Recombinant Full Length Dictyostelium Discoideum Adenosine 3'-Phospho 5'-Phosphosulfate Transporter 1(Slc35B2) Protein, His-Tagged E.coli Dictyostelium Discoideum His Full L. Full Length (1-359)
Slc35b2-2696M Recombinant Mouse Slc35b2 Protein, His&GST-tagged E.coli Mouse His&GST Asp2-Tyr295

    Involved Pathway

    SLC35B2 involved in several pathways and played different roles in them. We selected most pathways SLC35B2 participated on our site, such as Biological oxidations,Cytosolic sulfonation of small molecules,Glycosaminoglycan metabolism, which may be useful for your reference. Also, other proteins which involved in the same pathway with SLC35B2 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

    Pathway Name Pathway Related Protein
    Glycosaminoglycan metabolism VCANB,OMD,BGNB,HAS3,HPSE,KERA,MAPK1IP1L,CSPG5B,SLC26A2,HAS1
    Cytosolic sulfonation of small molecules SLC35B3,BPNT1,SULT2ST2,SLC26A2,ABHD14B,SULT1ST5,SULT1B1,SULT1ST6,SULT1C4,SLC26A1
    Metabolism of carbohydrates HPSE,LYVE1,HS3ST6,DSEL,SLC25A11,SLC25A12,Gpc2,KIAA1199,GYG1A,B3GNT3
    SLC-mediated transmembrane transport SLC34A2A,SLC6A7,SLC1A7A,SLC1A3B,SLC29A1A,SLC39A6,SLC39A10,SLC16A8,SLC44A5B,SLC6A20A
    Transmembrane transport of small molecules SLC2A8,SLC46A1,TRPC4A,TRPV3,SLC47A1,RHCGB,ASIC1A,SLC29A4,FXYD7,CLCN1
    Phase II conjugation UGT1B5,SULT2ST2,GLYATL2,ABHD14B,UGT1B2,AS3MT,Sult2a2,TPMT.2,SULT1B1,SULT4A1
    Biological oxidations CYP2C18,BPNT1,CYP3A5,UGT1B3,CYP19A1,CYP2K6,SLC35D1A,CYP27B1,CYP2B6,UGT1B1
    Metabolism CA5B,Sult2a2,GLTPA,PIK3R6,CYP2AD6,ACSF2,CYP2AD2,ST3GAL3A,ABHD10,SLC6A8

    Protein Function

    SLC35B2 has several biochemical functions, for example, 3-phosphoadenosine 5-phosphosulfate transmembrane transporter activity,signal transducer activity. Some of the functions are cooperated with other proteins, some of the functions could acted by SLC35B2 itself. We selected most functions SLC35B2 had, and list some proteins which have the same functions with SLC35B2. You can find most of the proteins on our site.

    Function Related Protein
    signal transducer activity TMTOPS2A,OLFR5,MTNR1BB,OLFCG3,LGR4,OLFR15,SLC44A2,CRKL,CTNNB2,OLFR150

    Interacting Protein

    SLC35B2 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with SLC35B2 here. Most of them are supplied by our site. Hope this information will be useful for your research of SLC35B2.

    MCTS1

    Resources

    References

    • Chim-Ong, A; Thawornkuno, C; et al. SLC35B2 Expression is Associated with a Poor Prognosis of Invasive Ductal Breast Carcinoma. ASIAN PACIFIC JOURNAL OF CANCER PREVENTION 15:6065-6070(2014).
    • Rosmarin, DM; Carette, JE; et al. Attachment of Chlamydia trachomatis L2 to host cells requires sulfation. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 109:10059-10064(2012).
    • de Andrea, CE; Prins, FA; et al. Growth plate regulation and osteochondroma formation: insights from tracing proteoglycans in zebrafish models and human cartilage. JOURNAL OF PATHOLOGY 224:160-168(2011).
    • Wiweger, MI; Avramut, CM; et al. Cartilage ultrastructure in proteoglycan-deficient zebrafish mutants brings to light new candidate genes for human skeletal disorders. JOURNAL OF PATHOLOGY 223:531-542(2011).

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