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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;
Species Cat.# Product name Source (Host) Tag Protein Length Price
Human SLC35B2-606HCL Recombinant Human SLC35B2 lysate HEK293 N/A
Mouse Slc35b2-2696M Recombinant Mouse Slc35b2 Protein, His&GST-tagged E.coli N-His&GST Asp2-Tyr295
Dictyostelium discoideum (Slime mold) RFL22028DF Recombinant Full Length Dictyostelium Discoideum Adenosine 3'-Phospho 5'-Phosphosulfate Transporter 1(Slc35B2) Protein, His-Tagged E.coli expression system His Full Length (1-359)
Zebrafish SLC35B2-11667Z Recombinant Zebrafish SLC35B2 Mammalian Cell His
  • Involved Pathway
  • Protein Function
  • Interacting Protein
  • SLC35B2 Related Articles

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
Biological oxidationsCYP3A7-CYP3AP1;CYP2U1;AHCY;CYP2AD2;UGT1B3;CYP4F12;GSTO2;CYP2K16;CYP2A13
Cytosolic sulfonation of small moleculesSULT1B1;SLC35B3;SULT2ST2;BPNT1;SULT1ST5;SULT1C2;Sult2a6;SLC35B2;SULT4A1
Glycosaminoglycan metabolismB3GNT2;UST;GPC5A;OGN;SLC35B2;HAS1;B3GNT3;KERA;B3GNT1
MetabolismABCA1;G0S2;NUDT3B;NUDT5;CLPS;CKB;NFYAL;GDF1;CYP8B2
Metabolism of carbohydratesCHST14;B3GNT2A;B3GNT3;HPSE;GYG1A;UST;CHST9;SLC5A2;HAS3
Phase II conjugationUGT1B7;SULT1B1;UGT1B5;SLC26A2;UGT1B2;GGTLC1;UGT1B1;GLYAT;BPNT1
SLC-mediated transmembrane transportSLC15A4;SLC7A3;SLC1A3A;SLC28A1;SLC3A2B;SLC5A11;SLC2A6;SLC30A6;SLC6A20B
Transmembrane transport of small moleculesTRPM4C;AQP1A.2;RHCG2A;AZGP1;ABCG2D;TRPV3;ATP1A1A.4;NIPA1;SLC2A13

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
3-phosphoadenosine 5-phosphosulfate transmembrane transporter activity
signal transducer activityTAAR8C;PTK2AA;OLFCW1;TRHR2;VMN1R49;TAS2R134;SLC20A1;TAAR12A;OLFR150

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

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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