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Protein

Carbohydrate sulfotransferase 14

Gene

CHST14

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

Functioni

Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of dermatan sulfate. Plays a pivotal role in the formation of 4-0-sulfated IdoA blocks in dermatan sulfate. Transfers sulfate to the C-4 hydroxyl of beta1,4-linked GalNAc that is substituted with an alpha-linked iduronic acid (IdoUA) at the C-3 hydroxyl. Transfers sulfate more efficiently to GalNAc residues in -IdoUA-GalNAc-IdoUA- than in -GlcUA-GalNAc-GlcUA-sequences. Has preference for partially desulfated dermatan sulfate. Addition of sulfate to GalNAc may occur immediately after epimerization of GlcUA to IdoUA. GlcUA to IdoUA. Appears to have an important role in the formation of the cerbellar neural network during postnatal brain development.1 Publication

Catalytic activityi

3'-phospho-5'-adenylyl sulfate + [dermatan]-N-acetyl-D-galactosamine = adenosine 3',5'-bisphosphate + [dermatan]- 4-O-sulfo-N-acetyl-D-galactosamine.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi155 – 1617PAPSBy similarity
Nucleotide bindingi213 – 2219PAPSBy similarity

GO - Molecular functioni

  • N-acetylgalactosamine 4-O-sulfotransferase activity Source: UniProtKB
  • phosphate ion binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000169105-MONOMER.
BRENDAi2.8.2.35. 2681.
ReactomeiR-HSA-2022923. Dermatan sulfate biosynthesis.
R-HSA-3595174. Defective CHST14 causes EDS, musculocontractural type.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbohydrate sulfotransferase 14 (EC:2.8.2.35)
Alternative name(s):
Dermatan 4-sulfotransferase 1
Short name:
D4ST-1
Short name:
hD4ST1
Gene namesi
Name:CHST14
Synonyms:D4ST1
ORF Names:UNQ1925/PRO4400
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:24464. CHST14.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3939CytoplasmicSequence analysisAdd
BLAST
Transmembranei40 – 6021Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini61 – 376316LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Ehlers-Danlos syndrome, musculocontractural type 1 (EDSMC1)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of Ehlers-Danlos syndrome characterized by distinctive craniofacial dysmorphism, congenital contractures of thumbs and fingers, clubfeet, severe kyphoscoliosis, muscular hypotonia, hyperextensible thin skin with easy bruisability and atrophic scarring, wrinkled palms, joint hypermobility, and ocular involvement.
See also OMIM:601776
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti135 – 1351R → G in EDSMC1; associated in a complex allele with Q-137; results in altered intracellular processing. 1 Publication
VAR_063754
Natural varianti137 – 1371L → Q in EDSMC1; associated in a complex allele with G-135; results in altered intracellular processing. 1 Publication
Corresponds to variant rs267606728 [ dbSNP | Ensembl ].
VAR_063755
Natural varianti213 – 2131R → P in EDSMC1; results in altered intracellular processing. 1 Publication
Corresponds to variant rs121908257 [ dbSNP | Ensembl ].
VAR_063756
Natural varianti281 – 2811P → L in EDSMC1; loss of activity. 1 Publication
Corresponds to variant rs267606729 [ dbSNP | Ensembl ].
VAR_064555
Natural varianti289 – 2891C → S in EDSMC1; loss of activity. 1 Publication
Corresponds to variant rs267606731 [ dbSNP | Ensembl ].
VAR_064556
Natural varianti293 – 2931Y → C in EDSMC1; results in altered intracellular processing; loss of activity. 2 Publications
Corresponds to variant rs121908258 [ dbSNP | Ensembl ].
VAR_063757

Keywords - Diseasei

Disease mutation, Ehlers-Danlos syndrome

Organism-specific databases

MalaCardsiCHST14.
MIMi601776. phenotype.
Orphaneti2953. Ehlers-Danlos syndrome, musculocontractural type.
PharmGKBiPA162382258.

Polymorphism and mutation databases

BioMutaiCHST14.
DMDMi61211839.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 376376Carbohydrate sulfotransferase 14PRO_0000189672Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi110 – 1101N-linked (GlcNAc...)Sequence analysis
Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiQ8NCH0.
MaxQBiQ8NCH0.
PaxDbiQ8NCH0.
PeptideAtlasiQ8NCH0.
PRIDEiQ8NCH0.

PTM databases

iPTMnetiQ8NCH0.
PhosphoSiteiQ8NCH0.

Expressioni

Tissue specificityi

Widely expressed. Expressed at high level in pituitary gland, placenta, uterus and thyroid.1 Publication

Gene expression databases

BgeeiQ8NCH0.
CleanExiHS_CHST14.
ExpressionAtlasiQ8NCH0. baseline and differential.
GenevisibleiQ8NCH0. HS.

Interactioni

Protein-protein interaction databases

BioGridi125232. 5 interactions.
STRINGi9606.ENSP00000307297.

Structurei

3D structure databases

ProteinModelPortaliQ8NCH0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfotransferase 2 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4651. Eukaryota.
ENOG4111GJR. LUCA.
GeneTreeiENSGT00760000119214.
HOGENOMiHOG000231801.
HOVERGENiHBG050954.
InParanoidiQ8NCH0.
KOiK08105.
OMAiMFPRPLT.
PhylomeDBiQ8NCH0.
TreeFamiTF325581.

Family and domain databases

InterProiIPR018011. Carb_sulfotransferase-rel.
IPR005331. Sulfotransferase.
[Graphical view]
PANTHERiPTHR12137. PTHR12137. 1 hit.
PfamiPF03567. Sulfotransfer_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8NCH0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFPRPLTPLA APNGAEPLGR ALRRAPLGRA RAGLGGPPLL LPSMLMFAVI
60 70 80 90 100
VASSGLLLMI ERGILAEMKP LPLHPPGREG TAWRGKAPKP GGLSLRAGDA
110 120 130 140 150
DLQVRQDVRN RTLRAVCGQP GMPRDPWDLP VGQRRTLLRH ILVSDRYRFL
160 170 180 190 200
YCYVPKVACS NWKRVMKVLA GVLDSVDVRL KMDHRSDLVF LADLRPEEIR
210 220 230 240 250
YRLQHYFKFL FVREPLERLL SAYRNKFGEI REYQQRYGAE IVRRYRAGAG
260 270 280 290 300
PSPAGDDVTF PEFLRYLVDE DPERMNEHWM PVYHLCQPCA VHYDFVGSYE
310 320 330 340 350
RLEADANQVL EWVRAPPHVR FPARQAWYRP ASPESLHYHL CSAPRALLQD
360 370
VLPKYILDFS LFAYPLPNVT KEACQQ
Length:376
Mass (Da):42,997
Last modified:March 15, 2005 - v2
Checksum:i53BF537979260188
GO

Sequence cautioni

The sequence AAQ88811.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti195 – 1951R → L in BAC11172 (PubMed:14702039).Curated
Sequence conflicti214 – 2141E → D in BAC11172 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti135 – 1351R → G in EDSMC1; associated in a complex allele with Q-137; results in altered intracellular processing. 1 Publication
VAR_063754
Natural varianti137 – 1371L → Q in EDSMC1; associated in a complex allele with G-135; results in altered intracellular processing. 1 Publication
Corresponds to variant rs267606728 [ dbSNP | Ensembl ].
VAR_063755
Natural varianti213 – 2131R → P in EDSMC1; results in altered intracellular processing. 1 Publication
Corresponds to variant rs121908257 [ dbSNP | Ensembl ].
VAR_063756
Natural varianti281 – 2811P → L in EDSMC1; loss of activity. 1 Publication
Corresponds to variant rs267606729 [ dbSNP | Ensembl ].
VAR_064555
Natural varianti289 – 2891C → S in EDSMC1; loss of activity. 1 Publication
Corresponds to variant rs267606731 [ dbSNP | Ensembl ].
VAR_064556
Natural varianti293 – 2931Y → C in EDSMC1; results in altered intracellular processing; loss of activity. 2 Publications
Corresponds to variant rs121908258 [ dbSNP | Ensembl ].
VAR_063757

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF401222 mRNA. Translation: AAK92532.1.
AB066595 mRNA. Translation: BAB84097.1.
AF282905 mRNA. Translation: AAK69530.1.
AK074739 mRNA. Translation: BAC11172.1.
BC023653 mRNA. Translation: AAH23653.1.
BC049214 mRNA. Translation: AAH49214.1.
BC053633 mRNA. Translation: AAH53633.1.
AY358446 mRNA. Translation: AAQ88811.1. Different initiation.
CCDSiCCDS10059.1.
RefSeqiNP_569735.1. NM_130468.3.
UniGeneiHs.442449.

Genome annotation databases

EnsembliENST00000306243; ENSP00000307297; ENSG00000169105.
GeneIDi113189.
KEGGihsa:113189.
UCSCiuc001zlw.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF401222 mRNA. Translation: AAK92532.1.
AB066595 mRNA. Translation: BAB84097.1.
AF282905 mRNA. Translation: AAK69530.1.
AK074739 mRNA. Translation: BAC11172.1.
BC023653 mRNA. Translation: AAH23653.1.
BC049214 mRNA. Translation: AAH49214.1.
BC053633 mRNA. Translation: AAH53633.1.
AY358446 mRNA. Translation: AAQ88811.1. Different initiation.
CCDSiCCDS10059.1.
RefSeqiNP_569735.1. NM_130468.3.
UniGeneiHs.442449.

3D structure databases

ProteinModelPortaliQ8NCH0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125232. 5 interactions.
STRINGi9606.ENSP00000307297.

PTM databases

iPTMnetiQ8NCH0.
PhosphoSiteiQ8NCH0.

Polymorphism and mutation databases

BioMutaiCHST14.
DMDMi61211839.

Proteomic databases

EPDiQ8NCH0.
MaxQBiQ8NCH0.
PaxDbiQ8NCH0.
PeptideAtlasiQ8NCH0.
PRIDEiQ8NCH0.

Protocols and materials databases

DNASUi113189.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000306243; ENSP00000307297; ENSG00000169105.
GeneIDi113189.
KEGGihsa:113189.
UCSCiuc001zlw.4. human.

Organism-specific databases

CTDi113189.
GeneCardsiCHST14.
HGNCiHGNC:24464. CHST14.
MalaCardsiCHST14.
MIMi601776. phenotype.
608429. gene.
neXtProtiNX_Q8NCH0.
Orphaneti2953. Ehlers-Danlos syndrome, musculocontractural type.
PharmGKBiPA162382258.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4651. Eukaryota.
ENOG4111GJR. LUCA.
GeneTreeiENSGT00760000119214.
HOGENOMiHOG000231801.
HOVERGENiHBG050954.
InParanoidiQ8NCH0.
KOiK08105.
OMAiMFPRPLT.
PhylomeDBiQ8NCH0.
TreeFamiTF325581.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000169105-MONOMER.
BRENDAi2.8.2.35. 2681.
ReactomeiR-HSA-2022923. Dermatan sulfate biosynthesis.
R-HSA-3595174. Defective CHST14 causes EDS, musculocontractural type.

Miscellaneous databases

ChiTaRSiCHST14. human.
GeneWikiiCHST14.
GenomeRNAii113189.
PROiQ8NCH0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8NCH0.
CleanExiHS_CHST14.
ExpressionAtlasiQ8NCH0. baseline and differential.
GenevisibleiQ8NCH0. HS.

Family and domain databases

InterProiIPR018011. Carb_sulfotransferase-rel.
IPR005331. Sulfotransferase.
[Graphical view]
PANTHERiPTHR12137. PTHR12137. 1 hit.
PfamiPF03567. Sulfotransfer_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of a dermatan-specific N-acetylgalactosamine 4-O-sulfotransferase."
    Evers M.R., Xia G., Kang H.-G., Schachner M., Baenziger J.U.
    J. Biol. Chem. 276:36344-36353(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY.
  2. "Specificities of three distinct human chondroitin/dermatan N-acetylgalactosamine 4-O-sulfotransferases demonstrated using partially desulfated dermatan sulfate as an acceptor. Implication of differential roles in dermatan sulfate biosynthesis."
    Mikami T., Mizumoto S., Kago N., Kitagawa H., Sugahara K.
    J. Biol. Chem. 278:36115-36127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBSTRATE SPECIFICITY.
  3. Hiraoka N., Fukuda M.
    Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Teratocarcinoma.
  5. "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].
    Tissue: Lung and Uterus.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-376.
  7. "Dermatan 4-O-sulfotransferase 1 is pivotal in the formation of iduronic acid blocks in dermatan sulfate."
    Pacheco B., Maccarana M., Malmstrom A.
    Glycobiology 19:1197-1203(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION.
  8. "Musculocontractural Ehlers-Danlos syndrome (former EDS type VIB) and adducted thumb clubfoot syndrome (ATCS) represent a single clinical entity caused by mutations in the dermatan-4-sulfotransferase 1 encoding CHST14 gene."
    Malfait F., Syx D., Vlummens P., Symoens S., Nampoothiri S., Hermanns-Le T., Van Laer L., De Paepe A.
    Hum. Mutat. 31:1233-1239(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN EDSMC1.
  9. Cited for: VARIANTS EDSMC1 GLY-135; GLN-137; PRO-213 AND CYS-293, CHARACTERIZATION OF VARIANTS EDSMC1 GLY-135; GLN-137; PRO-213 AND CYS-293.
  10. Cited for: VARIANTS EDSMC1 LEU-281; SER-289 AND CYS-293, CHARACTERIZATION OF VARIANTS EDSMC1 LEU-281; SER-289 AND CYS-293.

Entry informationi

Entry nameiCHSTE_HUMAN
AccessioniPrimary (citable) accession number: Q8NCH0
Secondary accession number(s): Q6PJ31, Q6UXA0, Q96P94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: July 6, 2016
This is version 113 of the entry and version 2 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 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.