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Protein

Carbohydrate sulfotransferase 14

Gene

Chst14

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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.1 Publication

Regions

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

BRENDAi2.8.2.35. 3474.
ReactomeiR-MMU-2022923. Dermatan sulfate biosynthesis.

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
Gene namesi
Name:Chst14
Synonyms:D4st1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1919386. 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

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 376376Carbohydrate sulfotransferase 14PRO_0000189673Add
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

MaxQBiQ80V53.
PaxDbiQ80V53.
PRIDEiQ80V53.

PTM databases

PhosphoSiteiQ80V53.

Expressioni

Developmental stagei

Low levels of expression in olfactory bulb, caudate putamen, cerebral cortex, hippocampus, thalamus, midbrain and cerebellum during early postnatal development. In later stages, exclusively expressed in cerebellum culminating at P14 of postnatal development.1 Publication

Gene expression databases

BgeeiQ80V53.
ExpressionAtlasiQ80V53. baseline and differential.
GenevisibleiQ80V53. MM.

Interactioni

Protein-protein interaction databases

IntActiQ80V53. 2 interactions.
MINTiMINT-218506.
STRINGi10090.ENSMUSP00000099579.

Structurei

3D structure databases

ProteinModelPortaliQ80V53.
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.
InParanoidiQ80V53.
KOiK08105.
OMAiMFPRPLT.
PhylomeDBiQ80V53.
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.

Q80V53-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFPRPLTPLA APKSAETLGR TPRRAPLGRA RAGLGGPPLL LPSMLMFAVI
60 70 80 90 100
VASSGLLLMI ERGILSEMKP LPLHPPSHKG AAWSGTDPKP RGLSLDAGDS
110 120 130 140 150
DLQVREDIRN RTLRAVCGQP GMPRDPWDLP VGQRRTLLRH ILVSDRYRFL
160 170 180 190 200
YCYVPKVACS NWKRVLKVLA GILNNVDVRL KMDHRSDLVF LADLRPEEIR
210 220 230 240 250
YRLQHYFKFL FVRDPLERLL SAYRNKFGEI REYQQRYGAE IVRRYRAGAG
260 270 280 290 300
PSPAGDDVTF PEFLRYLVDE DPEHMNEHWM PVYHLCQPCA VHYDFVGSYE
310 320 330 340 350
RLEADANQVL EWVRAPPHVR FPARQAWYRP ASPESLHYHL CNVPRALLQD
360 370
VLPKYILDFS LFAYPLPNVT KEACHQ
Length:376
Mass (Da):43,145
Last modified:March 15, 2005 - v2
Checksum:i319E5A82E3AA4ACF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti172 – 1721I → V in AAH43700 (PubMed:15489334).Curated
Sequence conflicti172 – 1721I → V in AAH26886 (PubMed:15489334).Curated
Sequence conflicti185 – 1851R → P in AAH43700 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011230 mRNA. Translation: BAB27480.1.
AK154636 mRNA. Translation: BAE32731.1.
AK159357 mRNA. Translation: BAE35015.1.
AK171614 mRNA. Translation: BAE42565.1.
AL845164 Genomic DNA. Translation: CAM19755.1.
BC026886 mRNA. Translation: AAH26886.1.
BC043700 mRNA. Translation: AAH43700.1.
BC085479 mRNA. Translation: AAH85479.1.
CCDSiCCDS16587.1.
RefSeqiNP_082393.3. NM_028117.3.
UniGeneiMm.486238.
Mm.490292.

Genome annotation databases

EnsembliENSMUST00000099546; ENSMUSP00000099579; ENSMUSG00000074916.
GeneIDi72136.
KEGGimmu:72136.
UCSCiuc012cbn.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011230 mRNA. Translation: BAB27480.1.
AK154636 mRNA. Translation: BAE32731.1.
AK159357 mRNA. Translation: BAE35015.1.
AK171614 mRNA. Translation: BAE42565.1.
AL845164 Genomic DNA. Translation: CAM19755.1.
BC026886 mRNA. Translation: AAH26886.1.
BC043700 mRNA. Translation: AAH43700.1.
BC085479 mRNA. Translation: AAH85479.1.
CCDSiCCDS16587.1.
RefSeqiNP_082393.3. NM_028117.3.
UniGeneiMm.486238.
Mm.490292.

3D structure databases

ProteinModelPortaliQ80V53.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ80V53. 2 interactions.
MINTiMINT-218506.
STRINGi10090.ENSMUSP00000099579.

PTM databases

PhosphoSiteiQ80V53.

Proteomic databases

MaxQBiQ80V53.
PaxDbiQ80V53.
PRIDEiQ80V53.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000099546; ENSMUSP00000099579; ENSMUSG00000074916.
GeneIDi72136.
KEGGimmu:72136.
UCSCiuc012cbn.1. mouse.

Organism-specific databases

CTDi113189.
MGIiMGI:1919386. Chst14.

Phylogenomic databases

eggNOGiKOG4651. Eukaryota.
ENOG4111GJR. LUCA.
GeneTreeiENSGT00760000119214.
HOGENOMiHOG000231801.
HOVERGENiHBG050954.
InParanoidiQ80V53.
KOiK08105.
OMAiMFPRPLT.
PhylomeDBiQ80V53.
TreeFamiTF325581.

Enzyme and pathway databases

BRENDAi2.8.2.35. 3474.
ReactomeiR-MMU-2022923. Dermatan sulfate biosynthesis.

Miscellaneous databases

PROiQ80V53.
SOURCEiSearch...

Gene expression databases

BgeeiQ80V53.
ExpressionAtlasiQ80V53. baseline and differential.
GenevisibleiQ80V53. MM.

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. "Chondroitin sulfate/dermatan sulfate hybrid chains in the development of cerebellum. Spatiotemporal regulation of the expression of critical disulfated disaccharides by specific sulfotransferases."
    Mitsunaga C., Mikami T., Mizumoto S., Fukuda J., Sugahara K.
    J. Biol. Chem. 281:18942-18952(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, FUNCTION, ENZYME ACTIVITY.
    Tissue: Heart.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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].
    Strain: C57BL/6J and FVB/N.
    Tissue: Brain and Mammary gland.

Entry informationi

Entry nameiCHSTE_MOUSE
AccessioniPrimary (citable) accession number: Q80V53
Secondary accession number(s): A2AQV3
, Q3TXA1, Q8R304, Q9D0P2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: June 8, 2016
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.