SCUBA

CHST15 — Carbohydrate sulfotransferase 15

CHST15 belongs to a gene co-expression module in 5 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.

CHST15's module in each cell type

Cell typeModuleShares the module with
EndothelialInflammatory Angiogenesis
ECM remodeling
ADM, APOD, CMTM3, GPIHBP1, GRAP, HOMER3, LOX, MYH10 +7 moreView in SCUBA
FibroblastsInflammatory Fibroblast Activation
Inflammatory
ALPL, ARL4C, CD44, CXCL6, DCBLD1, EVA1A, MAP3K5, MICALL2 +4 moreView in SCUBA
Lymphatic endothelialLymphatic EC Identity
Gut residence
CD36, CERS6, DOCK5, EPS15, FRMD4B, FRY, IL7, ITSN1 +4 moreView in SCUBA
MacrophagesRAB-mediated Trafficking
Vesicular traficking
ABI1, ACSL3, ARMC8, CACUL1, CD86, CRTC3, CTNNA1, CUL4A +27 moreView in SCUBA
NeutrophilsTLR2 Innate Signaling
Innate immunity
AATK, CYRIA, DHX34, ECE1, ERGIC1, MAP4K4, MKNK1, STK40 +4 more

About the gene

SynonymsBRAG, GALNAC4S-6ST, KIAA0598
Chromosome10: 124007668-124093598
Predicted locationIntracellular, Membrane
Essential geneNo
Protein classEnzymes, Metabolic proteins, Predicted intracellular proteins, Predicted membrane proteins
Molecular functionTransferase

Function

Sulfotransferase that transfers sulfate from 3'- phosphoadenosine 5'-phosphosulfate (PAPS) to the C-6 hydroxyl group of the GalNAc 4-sulfate residue of chondroitin sulfate A and forms chondroitin sulfate E containing GlcA-GalNAc(4,6-SO(4)) repeating units. It also transfers sulfate to a unique non-reducing terminal sequence, GalNAc(4SO4)-GlcA(2SO4)-GalNAc(6SO4), to yield a highly sulfated structure similar to the structure found in thrombomodulin chondroitin sulfate. May also act as a B-cell receptor involved in BCR ligation-mediated early activation that mediate regulatory signals key to B-cell development and/or regulation of B-cell-specific RAG expression; however such results are unclear in vivo

Human Protein Atlas · Open Targets · UniProt

Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.