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Protein

Carbohydrate sulfotransferase 15

Gene

CHST15

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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-SO4) 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.2 Publications

Catalytic activityi

3-phospho-5-adenylyl sulfate + [dermatan]-4-O-sulfo-N-acetylgalactosamine = adenosine 3',5'-bisphosphate + [dermatan]-4,6-di-O-sulfo-N-acetyl-D-galactosamine.1 Publication
3-phospho-5-adenylyl sulfate + [chondroitin]-4-O-sulfo-N-acetylgalactosamine = adenosine 3',5'-bisphosphate + [chondroitin]-4,6-di-O-sulfo-N-acetyl-D-galactosamine.1 Publication

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Inhibited by phenyl beta-GalNAc(4,6-SO4).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei392 – 3921PAPSBy similarity
Binding sitei400 – 4001PAPSBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi263 – 2675PAPSBy similarity

GO - Molecular functioni

  • 3'-phosphoadenosine 5'-phosphosulfate binding Source: UniProtKB
  • N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase activity Source: UniProtKB

GO - Biological processi

  • chondroitin sulfate biosynthetic process Source: Reactome
  • hexose biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciMetaCyc:HS11694-MONOMER.
BRENDAi2.8.2.33. 2681.
ReactomeiR-HSA-2022870. Chondroitin sulfate biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbohydrate sulfotransferase 15 (EC:2.8.2.33)
Alternative name(s):
B-cell RAG-associated gene protein
Short name:
hBRAG
N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase
Short name:
GalNAc4S-6ST
Gene namesi
Name:CHST15
Synonyms:BRAG, GALNAC4S6ST, KIAA0598
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:18137. CHST15.

Subcellular locationi

  • Golgi apparatus membrane 1 Publication; Single-pass type II membrane protein 1 Publication

  • Note: A small fraction may also be present at the cell surface, where it acts as a B-cell receptor.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 8080CytoplasmicSequence analysisAdd
BLAST
Transmembranei81 – 10121Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini102 – 561460LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

  • Golgi membrane Source: Reactome
  • integral component of membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165548385.

Polymorphism and mutation databases

DMDMi74749920.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 561561Carbohydrate sulfotransferase 15PRO_0000225623Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi364 – 3641N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ7LFX5.
PeptideAtlasiQ7LFX5.
PRIDEiQ7LFX5.

PTM databases

iPTMnetiQ7LFX5.
PhosphoSiteiQ7LFX5.

Expressioni

Tissue specificityi

Expressed in B-cell-enriched tissues but not in fetal or adult thymus. Expressed in fetal and adult spleen, lymph node, tonsil, bone marrow and peripheral leukocytes. Not expressed in T-cells. In pro-B, pre-B, and mature B-cell lines, it colocalizes with RAG1.1 Publication

Gene expression databases

BgeeiQ7LFX5.
ExpressionAtlasiQ7LFX5. baseline and differential.
GenevisibleiQ7LFX5. HS.

Organism-specific databases

HPAiHPA017584.

Interactioni

Subunit structurei

Homodimer; disulfide-linked (Potential). The relevance of homodimerization is however unsure. May interact with phosphorylated proteins in resting B-cells, including HCK.Curated1 Publication

Protein-protein interaction databases

BioGridi119498. 22 interactions.
IntActiQ7LFX5. 19 interactions.
STRINGi9606.ENSP00000333947.

Structurei

3D structure databases

ProteinModelPortaliQ7LFX5.
SMRiQ7LFX5. Positions 254-559.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfotransferase 1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IISS. Eukaryota.
ENOG410XSMU. LUCA.
GeneTreeiENSGT00390000004719.
HOGENOMiHOG000154435.
InParanoidiQ7LFX5.
KOiK08106.
OMAiHASNVKY.
OrthoDBiEOG7QC7ZD.
PhylomeDBiQ7LFX5.
TreeFamiTF333516.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q7LFX5-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRHCINCCIQ LLPDGAHKQQ VNCQGGPHHG HQACPTCKGE NKILFRVDSK
60 70 80 90 100
QMNLLAVLEV RTEGNENWGG FLRFKKGKRC SLVFGLIIMT LVMASYILSG
110 120 130 140 150
AHQELLISSP FHYGGFPSNP SLMDSENPSD TKEHHHQSSV NNISYMKDYP
160 170 180 190 200
SIKLIINSIT TRIEFTTRQL PDLEDLKKQE LHMFSVIPNK FLPNSKSPCW
210 220 230 240 250
YEEFSGQNTT DPYLTNSYVL YSKRFRSTFD ALRKAFWGHL AHAHGKHFRL
260 270 280 290 300
RCLPHFYIIG QPKCGTTDLY DRLRLHPEVK FSAIKEPHWW TRKRFGIVRL
310 320 330 340 350
RDGLRDRYPV EDYLDLFDLA AHQIHQGLQA SSAKEQSKMN TIIIGEASAS
360 370 380 390 400
TMWDNNAWTF FYDNSTDGEP PFLTQDFIHA FQPNARLIVM LRDPVERLYS
410 420 430 440 450
DYLYFASSNK SADDFHEKVT EALQLFENCM LDYSLRACVY NNTLNNAMPV
460 470 480 490 500
RLQVGLYAVY LLDWLSVFDK QQFLILRLED HASNVKYTMH KVFQFLNLGP
510 520 530 540 550
LSEKQEALMT KSPASNARRP EDRNLGPMWP ITQKILRDFY RPFNARLAQV
560
LADEAFAWKT T
Length:561
Mass (Da):64,926
Last modified:July 5, 2004 - v1
Checksum:i74643A7CFF7F242D
GO
Isoform 2 (identifier: Q7LFX5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     451-561: RLQVGLYAVY...ADEAFAWKTT → CTPPPRTPRA...PLFMDVKAEN

Note: No experimental confirmation available.
Show »
Length:506
Mass (Da):58,109
Checksum:iFD022040B4DB2920
GO

Sequence cautioni

The sequence AAC71691.1 differs from that shown. Reason: Frameshift at positions 180, 223, 489 and 537. Curated
The sequence AAH50540.1 differs from that shown. Reason: Frameshift at position 511. Curated
The sequence BAA25524.2 differs from that shown. Reason: Erroneous initiation. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei451 – 561111RLQVG…AWKTT → CTPPPRTPRAGPWQKELVCC YYASGIVGLRFSIGTERSVL MCKCCSPLFMDVKAEN in isoform 2. 1 PublicationVSP_017387Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF026477 mRNA. Translation: AAC71691.1. Frameshift.
AB025341 Genomic DNA. Translation: BAA83686.1.
AB062423 mRNA. Translation: BAB72145.1.
AB011170 mRNA. Translation: BAA25524.2. Different initiation.
CR749804 mRNA. Translation: CAH18664.1.
AL683842 Genomic DNA. Translation: CAI14442.1.
BC027908 mRNA. Translation: AAH27908.1.
BC050540 mRNA. Translation: AAH50540.1. Frameshift.
BC075813 mRNA. Translation: AAH75813.1.
CCDSiCCDS55731.1. [Q7LFX5-2]
CCDS7638.1. [Q7LFX5-1]
RefSeqiNP_001257693.1. NM_001270764.1. [Q7LFX5-1]
NP_001257694.1. NM_001270765.1. [Q7LFX5-2]
NP_056976.2. NM_015892.4. [Q7LFX5-1]
XP_005269948.1. XM_005269891.2. [Q7LFX5-1]
XP_006717954.1. XM_006717891.2. [Q7LFX5-1]
UniGeneiHs.287537.
Hs.745222.

Genome annotation databases

EnsembliENST00000346248; ENSP00000333947; ENSG00000182022. [Q7LFX5-1]
ENST00000435907; ENSP00000402394; ENSG00000182022. [Q7LFX5-1]
ENST00000628426; ENSP00000485905; ENSG00000182022. [Q7LFX5-2]
GeneIDi51363.
KEGGihsa:51363.
UCSCiuc001lhm.5. human. [Q7LFX5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF026477 mRNA. Translation: AAC71691.1. Frameshift.
AB025341 Genomic DNA. Translation: BAA83686.1.
AB062423 mRNA. Translation: BAB72145.1.
AB011170 mRNA. Translation: BAA25524.2. Different initiation.
CR749804 mRNA. Translation: CAH18664.1.
AL683842 Genomic DNA. Translation: CAI14442.1.
BC027908 mRNA. Translation: AAH27908.1.
BC050540 mRNA. Translation: AAH50540.1. Frameshift.
BC075813 mRNA. Translation: AAH75813.1.
CCDSiCCDS55731.1. [Q7LFX5-2]
CCDS7638.1. [Q7LFX5-1]
RefSeqiNP_001257693.1. NM_001270764.1. [Q7LFX5-1]
NP_001257694.1. NM_001270765.1. [Q7LFX5-2]
NP_056976.2. NM_015892.4. [Q7LFX5-1]
XP_005269948.1. XM_005269891.2. [Q7LFX5-1]
XP_006717954.1. XM_006717891.2. [Q7LFX5-1]
UniGeneiHs.287537.
Hs.745222.

3D structure databases

ProteinModelPortaliQ7LFX5.
SMRiQ7LFX5. Positions 254-559.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119498. 22 interactions.
IntActiQ7LFX5. 19 interactions.
STRINGi9606.ENSP00000333947.

PTM databases

iPTMnetiQ7LFX5.
PhosphoSiteiQ7LFX5.

Polymorphism and mutation databases

DMDMi74749920.

Proteomic databases

PaxDbiQ7LFX5.
PeptideAtlasiQ7LFX5.
PRIDEiQ7LFX5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000346248; ENSP00000333947; ENSG00000182022. [Q7LFX5-1]
ENST00000435907; ENSP00000402394; ENSG00000182022. [Q7LFX5-1]
ENST00000628426; ENSP00000485905; ENSG00000182022. [Q7LFX5-2]
GeneIDi51363.
KEGGihsa:51363.
UCSCiuc001lhm.5. human. [Q7LFX5-1]

Organism-specific databases

CTDi51363.
GeneCardsiCHST15.
HGNCiHGNC:18137. CHST15.
HPAiHPA017584.
MIMi608277. gene.
neXtProtiNX_Q7LFX5.
PharmGKBiPA165548385.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IISS. Eukaryota.
ENOG410XSMU. LUCA.
GeneTreeiENSGT00390000004719.
HOGENOMiHOG000154435.
InParanoidiQ7LFX5.
KOiK08106.
OMAiHASNVKY.
OrthoDBiEOG7QC7ZD.
PhylomeDBiQ7LFX5.
TreeFamiTF333516.

Enzyme and pathway databases

BioCyciMetaCyc:HS11694-MONOMER.
BRENDAi2.8.2.33. 2681.
ReactomeiR-HSA-2022870. Chondroitin sulfate biosynthesis.

Miscellaneous databases

ChiTaRSiCHST15. human.
GeneWikiiGALNAC4S-6ST.
GenomeRNAii51363.
PROiQ7LFX5.
SOURCEiSearch...

Gene expression databases

BgeeiQ7LFX5.
ExpressionAtlasiQ7LFX5. baseline and differential.
GenevisibleiQ7LFX5. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "hBRAG, a novel B cell lineage cDNA encoding a type II transmembrane glycoprotein potentially involved in the regulation of recombination activating gene 1 (RAG1)."
    Verkoczy L.K., Marsden P.A., Berinstein N.L.
    Eur. J. Immunol. 28:2839-2853(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Pre-B cell.
  2. "Structure, expression and mutational analysis of the hBRAG gene on 10q in the frequently deleted region in human endometrial cancer."
    Yuki M., Yoshinaga K., Yamakawa H., Sakurada K., Sato S., Yajima A., Horii A.
    Oncol. Rep. 7:1339-1342(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Human N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase cDNA is related to human B cell recombination activating gene-associated gene."
    Ohtake S., Ito Y., Fukuta M., Habuchi O.
    J. Biol. Chem. 276:43894-43900(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
    Tissue: Brain.
  4. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Blood, Duodenum and Lung.
  8. "Characterization of the human B cell RAG-associated gene, hBRAG, as a B cell receptor signal-enhancing glycoprotein dimer that associates with phosphorylated proteins in resting B cells."
    Verkoczy L.K., Guinn B.-A., Berinstein N.L.
    J. Biol. Chem. 275:20967-20979(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION, DISULFIDE BOND, INTERACTION WITH HCK.
  9. "A unique nonreducing terminal modification of chondroitin sulfate by N-acetylgalactosamine 4-sulfate 6-o-sulfotransferase."
    Ohtake S., Kimata K., Habuchi O.
    J. Biol. Chem. 278:38443-38452(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  10. "Synthesis of sulfated phenyl 2-acetamido-2-deoxy-D--D-galactopyranosides. 4-O-Sulfated phenyl 2-acetamido-2-deoxy-beta-D-galactopyranoside is a competitive acceptor that decreases sulfation of chondroitin sulfate by N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase."
    Sawada T., Fujii S., Nakano H., Ohtake S., Kimata K., Habuchi O.
    Carbohydr. Res. 340:1983-1996(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiCHSTF_HUMAN
AccessioniPrimary (citable) accession number: Q7LFX5
Secondary accession number(s): O60338, O60474, Q86VM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: July 5, 2004
Last modified: July 6, 2016
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.