SLC35B2
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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 |
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SLC35B2-11667Z | Recombinant Zebrafish SLC35B2 | Mammalian Cells | Zebrafish | His |
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SLC35B2-606HCL | Recombinant Human SLC35B2 lysate | HEK293 | Human | Non |
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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) |
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Slc35b2-2696M | Recombinant Mouse Slc35b2 Protein, His&GST-tagged | E.coli | Mouse | His&GST | Asp2-Tyr295 |
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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 |
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Phase II conjugation | GGTLC1,SULT1C4,GLYATL2,GLYAT,UGT1B5,SULT1B1,UGT1B3,SULT1ST5,SLC35D1A,SULT1ST6 |
SLC-mediated transmembrane transport | SLC7A11,SLC15A2,SLC24A6,SLC9A3.2,SLC22A7,SLC4A1B,SLC31A1,SLC13A4,SLC16A1,SLC1A2A |
Transmembrane transport of small molecules | SLC9B2,FXYD7,SLC39A2,LCN1,SLC9A9,TRPC4APB,CTNS,SLC9A7,BSND,NIPAL3 |
Cytosolic sulfonation of small molecules | SULT1ST6,BPNT1,Sult2a6,SULT1C2,SULT1B1,ABHD14B,SLC26A2,SLC35B3,SULT1C4,SULT1ST5 |
Glycosaminoglycan metabolism | SLC26A2,DSEL,KERA,KIAA1199,B3GAT2,HAS3,STAB2,SLC35B3,LYVE1,OMD |
Metabolism | MTP,CRAT,CKB,HS3ST6,ALOX5AP,CYP11B1,AQP1A.2,PDP2,FABP11A,SLCO1B1 |
Biological oxidations | CYP8B2,CYP4T8,Sult2a2,CYP21A2,COMT,CES1,ADH4,GSTO2,CYP2J2,ABHD10 |
Metabolism of carbohydrates | B3GNT1,HAS1,B3GAT2,SLC5A4,SLC5A2,SLC5A9,DSEL,HS3ST4,OMD,KIAA1199 |
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 |
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signal transducer activity | GNG5,GNB5,FPR-RS4,RGS9B,CXCR4A,PLCH2,OPN1MW4,TAS2R104,OLFR15,MAPKAPK2B |
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.
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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).