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Protein

Carbohydrate sulfotransferase 12

Gene

CHST12

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 chondroitin and desulfated dermatan sulfate. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Activity toward partially desulfated dermatan sulfate is however lower. Does not form 4, 6-di-O-sulfated GalNAc when chondroitin sulfate C is used as an acceptor.

Catalytic activityi

3'-phosphoadenylyl sulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 4'-sulfate.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi171 – 1777PAPSBy similarity
Nucleotide bindingi245 – 2539PAPSBy similarity

GO - Molecular functioni

  • 3'-phosphoadenosine 5'-phosphosulfate binding Source: UniProtKB
  • chondroitin 4-sulfotransferase activity Source: UniProtKB

GO - Biological processi

  • carbohydrate biosynthetic process Source: InterPro
  • chondroitin sulfate biosynthetic process Source: UniProtKB
  • dermatan sulfate biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

BioCyciMetaCyc:HS06130-MONOMER.
BRENDAi2.8.2.5. 2681.
ReactomeiR-HSA-2022870. Chondroitin sulfate biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbohydrate sulfotransferase 12 (EC:2.8.2.5)
Alternative name(s):
Chondroitin 4-O-sulfotransferase 2
Chondroitin 4-sulfotransferase 2
Short name:
C4ST-2
Short name:
C4ST2
Sulfotransferase Hlo
Gene namesi
Name:CHST12
ORF Names:UNQ500/PRO1017
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:17423. CHST12.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 55CytoplasmicSequence analysis
Transmembranei6 – 2621Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini27 – 414388LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134969008.

Polymorphism and mutation databases

BioMutaiCHST12.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 414414Carbohydrate sulfotransferase 12PRO_0000189668Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi134 – 1341N-linked (GlcNAc...)Sequence analysis
Glycosylationi209 – 2091N-linked (GlcNAc...)Sequence analysis
Glycosylationi280 – 2801N-linked (GlcNAc...)Sequence analysis
Glycosylationi370 – 3701N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiQ9NRB3.
MaxQBiQ9NRB3.
PaxDbiQ9NRB3.
PRIDEiQ9NRB3.

PTM databases

iPTMnetiQ9NRB3.
PhosphoSiteiQ9NRB3.

Expressioni

Tissue specificityi

Widely expressed. Expressed a high level in spinal chord, heart, spleen, thyroid, pituitary gland, adrenal gland, peripheral blood leukocytes, thymus, lung, small intestine, fetal kidney, fetal spleen and fetal lung.1 Publication

Gene expression databases

BgeeiQ9NRB3.
CleanExiHS_CHST12.
ExpressionAtlasiQ9NRB3. baseline and differential.
GenevisibleiQ9NRB3. HS.

Organism-specific databases

HPAiHPA041680.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
UGGT1Q9NYU21EBI-1042837,EBI-1056389

Protein-protein interaction databases

BioGridi120681. 24 interactions.
IntActiQ9NRB3. 3 interactions.
STRINGi9606.ENSP00000258711.

Structurei

3D structure databases

ProteinModelPortaliQ9NRB3.
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.
HOVERGENiHBG097841.
InParanoidiQ9NRB3.
KOiK04742.
OMAiDIPNYEL.
OrthoDBiEOG7B05D8.
PhylomeDBiQ9NRB3.
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.

Q9NRB3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKARLFRLW LVLGSVFMIL LIIVYWDSAG AAHFYLHTSF SRPHTGPPLP
60 70 80 90 100
TPGPDRDREL TADSDVDEFL DKFLSAGVKQ SDLPRKETEQ PPAPGSMEES
110 120 130 140 150
VRGYDWSPRD ARRSPDQGRQ QAERRSVLRG FCANSSLAFP TKERAFDDIP
160 170 180 190 200
NSELSHLIVD DRHGAIYCYV PKVACTNWKR VMIVLSGSLL HRGAPYRDPL
210 220 230 240 250
RIPREHVHNA SAHLTFNKFW RRYGKLSRHL MKVKLKKYTK FLFVRDPFVR
260 270 280 290 300
LISAFRSKFE LENEEFYRKF AVPMLRLYAN HTSLPASARE AFRAGLKVSF
310 320 330 340 350
ANFIQYLLDP HTEKLAPFNE HWRQVYRLCH PCQIDYDFVG KLETLDEDAA
360 370 380 390 400
QLLQLLQVDR QLRFPPSYRN RTASSWEEDW FAKIPLAWRQ QLYKLYEADF
410
VLFGYPKPEN LLRD
Length:414
Mass (Da):48,414
Last modified:March 15, 2005 - v2
Checksum:i8730D8731F623078
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301G → S in AAF81692 (PubMed:10781601).Curated
Sequence conflicti42 – 421R → K in AAF81692 (PubMed:10781601).Curated
Sequence conflicti92 – 921P → L in AAF81692 (PubMed:10781601).Curated
Sequence conflicti380 – 3801W → C in AAF81692 (PubMed:10781601).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti52 – 521P → H.
Corresponds to variant rs3735099 [ dbSNP | Ensembl ].
VAR_021471
Natural varianti61 – 611T → S.
Corresponds to variant rs3735100 [ dbSNP | Ensembl ].
VAR_021472
Natural varianti94 – 941P → L.
Corresponds to variant rs12536223 [ dbSNP | Ensembl ].
VAR_033738
Natural varianti109 – 1091R → S.
Corresponds to variant rs17132395 [ dbSNP | Ensembl ].
VAR_021473
Natural varianti145 – 1451A → P.
Corresponds to variant rs17132399 [ dbSNP | Ensembl ].
VAR_021474

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF239822 mRNA. Translation: AAF81692.1.
AJ289131 mRNA. Translation: CAB92133.1.
AY358574 mRNA. Translation: AAQ88937.1.
AK313484 mRNA. Translation: BAG36268.1.
CH236953 Genomic DNA. Translation: EAL23955.1.
BC002918 mRNA. Translation: AAH02918.1.
BC095492 mRNA. Translation: AAH95492.1.
CCDSiCCDS5333.1.
RefSeqiNP_001230723.1. NM_001243794.1.
NP_001230724.1. NM_001243795.1.
NP_061111.1. NM_018641.4.
XP_011513745.1. XM_011515443.1.
XP_011513746.1. XM_011515444.1.
UniGeneiHs.744987.

Genome annotation databases

EnsembliENST00000258711; ENSP00000258711; ENSG00000136213.
ENST00000618655; ENSP00000481912; ENSG00000136213.
GeneIDi55501.
KEGGihsa:55501.
UCSCiuc003smc.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF239822 mRNA. Translation: AAF81692.1.
AJ289131 mRNA. Translation: CAB92133.1.
AY358574 mRNA. Translation: AAQ88937.1.
AK313484 mRNA. Translation: BAG36268.1.
CH236953 Genomic DNA. Translation: EAL23955.1.
BC002918 mRNA. Translation: AAH02918.1.
BC095492 mRNA. Translation: AAH95492.1.
CCDSiCCDS5333.1.
RefSeqiNP_001230723.1. NM_001243794.1.
NP_001230724.1. NM_001243795.1.
NP_061111.1. NM_018641.4.
XP_011513745.1. XM_011515443.1.
XP_011513746.1. XM_011515444.1.
UniGeneiHs.744987.

3D structure databases

ProteinModelPortaliQ9NRB3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120681. 24 interactions.
IntActiQ9NRB3. 3 interactions.
STRINGi9606.ENSP00000258711.

PTM databases

iPTMnetiQ9NRB3.
PhosphoSiteiQ9NRB3.

Polymorphism and mutation databases

BioMutaiCHST12.

Proteomic databases

EPDiQ9NRB3.
MaxQBiQ9NRB3.
PaxDbiQ9NRB3.
PRIDEiQ9NRB3.

Protocols and materials databases

DNASUi55501.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000258711; ENSP00000258711; ENSG00000136213.
ENST00000618655; ENSP00000481912; ENSG00000136213.
GeneIDi55501.
KEGGihsa:55501.
UCSCiuc003smc.4. human.

Organism-specific databases

CTDi55501.
GeneCardsiCHST12.
HGNCiHGNC:17423. CHST12.
HPAiHPA041680.
MIMi610129. gene.
neXtProtiNX_Q9NRB3.
PharmGKBiPA134969008.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4651. Eukaryota.
ENOG4111GJR. LUCA.
GeneTreeiENSGT00760000119214.
HOGENOMiHOG000231801.
HOVERGENiHBG097841.
InParanoidiQ9NRB3.
KOiK04742.
OMAiDIPNYEL.
OrthoDBiEOG7B05D8.
PhylomeDBiQ9NRB3.
TreeFamiTF325581.

Enzyme and pathway databases

BioCyciMetaCyc:HS06130-MONOMER.
BRENDAi2.8.2.5. 2681.
ReactomeiR-HSA-2022870. Chondroitin sulfate biosynthesis.

Miscellaneous databases

ChiTaRSiCHST12. human.
GeneWikiiCHST12.
GenomeRNAii55501.
PROiQ9NRB3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NRB3.
CleanExiHS_CHST12.
ExpressionAtlasiQ9NRB3. baseline and differential.
GenevisibleiQ9NRB3. 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 expression of two distinct human chondroitin 4-O-sulfotransferases that belong to the HNK-1 sulfotransferase gene family."
    Hiraoka N., Nakagawa H., Ong E., Akama O.T., Fukuda N.M., Fukuda M.
    J. Biol. Chem. 275:20188-20196(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY.
  2. "Cloning and expression of molecules homologous to HNK-1 sulfotransferase."
    Xia G., Evers M.R., Schachner M.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE 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: Colon.
  5. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Brain and Skin.
  7. "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: SUBSTRATE SPECIFICITY.

Entry informationi

Entry nameiCHSTC_HUMAN
AccessioniPrimary (citable) accession number: Q9NRB3
Secondary accession number(s): A4D1Z9, Q502W3, Q9NXY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: June 8, 2016
This is version 115 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 7
    Human chromosome 7: 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.