Q9NPF2 (CHSTB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Carbohydrate sulfotransferase 11
EC=2.8.2.5

Alternative name(s):
Chondroitin 4-O-sulfotransferase 1
Chondroitin 4-sulfotransferase 1
Short name=C4S-1
Short name=C4ST-1
Short name=C4ST1

Gene names

Name:

CHST11

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	352 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Can also sulfate Gal residues in desulfated dermatan sulfate. Preferentially sulfates in GlcA->GalNAc unit than in IdoA->GalNAc unit. Does not form 4, 6-di-O-sulfated GalNAc when chondroitin sulfate C is used as an acceptor.
Catalytic activity	3'-phosphoadenylyl sulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 4'-sulfate. Ref.1 Ref.2
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein By similarity.
Tissue specificity	Widely expressed. Highly expressed in spleen, thymus, bone marrow, peripheral blood leukocytes, lymph node, heart, brain, lung and placenta. Ref.1 Ref.2
Post-translational modification	N-glycosylated; required for activity and stability. Ref.9
Involvement in disease	A chromosomal aberration involving CHST11 is found in B-cell chronic lymphocytic leukemias. Translocation t(12;14)(q23;q32) with IgH. Ref.8
Sequence similarities	Belongs to the sulfotransferase 2 family.
Biophysicochemical properties	Kinetic parameters: KM=0.5 µM for PAPS Ref.9 KM=2.1 mM for chondroitin

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing Chromosomal rearrangement
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate biosynthetic process Inferred from electronic annotation. Source: InterPro carbohydrate metabolic process Traceable author statement. Source: Reactome chondrocyte development Inferred from electronic annotation. Source: Compara chondroitin sulfate biosynthetic process Inferred from direct assay Ref.1. Source: UniProtKB developmental growth Inferred from electronic annotation. Source: Compara embryonic digit morphogenesis Inferred from electronic annotation. Source: Compara embryonic viscerocranium morphogenesis Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of transforming growth factor beta receptor signaling pathway Inferred from electronic annotation. Source: Compara polysaccharide localization Inferred from electronic annotation. Source: Compara post-anal tail morphogenesis Inferred from electronic annotation. Source: Compara post-embryonic development Inferred from electronic annotation. Source: Compara regulation of cell proliferation Inferred from electronic annotation. Source: Compara respiratory gaseous exchange Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi membrane Traceable author statement. Source: Reactome integral to membrane Non-traceable author statement Ref.1. Source: UniProtKB
Molecular_function	N-acetylgalactosamine 4-O-sulfotransferase activity Inferred from direct assay Ref.1. Source: UniProtKB N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase activity Inferred from electronic annotation. Source: Compara chondroitin 4-sulfotransferase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NPF2-1)

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.

Isoform 2 (identifier: Q9NPF2-2)

Also known as: C4S-1A;

The sequence of this isoform differs from the canonical sequence as follows:
     35-40: SMLHPV → I

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 352	352	Carbohydrate sulfotransferase 11		PRO_0000189664
Regions
	Topological domain	1 – 16	16	Cytoplasmic Potential
	Transmembrane	17 – 37	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	38 – 352	315	Lumenal Potential
	Nucleotide binding	124 – 130	7	PAPS By similarity
	Nucleotide binding	186 – 194	9	PAPS By similarity
Amino acid modifications
	Glycosylation	205	1	N-linked (GlcNAc...) Potential
	Glycosylation	223	1	N-linked (GlcNAc...) Potential
	Glycosylation	321	1	N-linked (GlcNAc...) Potential
	Glycosylation	342	1	N-linked (GlcNAc...) Probable
Natural variations
	Alternative sequence	35 – 40	6	SMLHPV → I in isoform 2.		VSP_012992
Experimental info
	Mutagenesis	125	1	K → Q: Abolishes enzyme activity but does not affect stability of the protein. Ref.9
	Mutagenesis	205	1	N → S: Induces a weak decrease in enzyme activity but has no effect on stability of the protein. Unstable protein; when associated with S-223 and S-321. Ref.9
	Mutagenesis	223	1	N → S: Induces a weak decrease in enzyme activity but has no effect on stability of the protein. Unstable protein; when associated with S-205 and S-321. Ref.9
	Mutagenesis	321	1	N → S: Induces a strong decrease in enzyme activity but has no effect on stability of the protein. Unstable protein; when associated with S-205 and S-223.
	Mutagenesis	342	1	N → S: Induces a strong decrease in enzyme activity has no effect on stability of the protein. Ref.9
	Sequence conflict	289	1	V → F in CAB87380. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 55DF1D29D6703307	FASTA	352	41,555
	10 20 30 40 50 60 MKPALLEVMR MNRICRMVLA TCLGSFILVI FYFQSMLHPV MRRNPFGVDI CCRKGSRSPL 70 80 90 100 110 120 QELYNPIQLE LSNTAVLHQM RRDQVTDTCR ANSATSRKRR VLTPNDLKHL VVDEDHELIY 130 140 150 160 170 180 CYVPKVACTN WKRLMMVLTG RGKYSDPMEI PANEAHVSAN LKTLNQYSIP EINHRLKSYM 190 200 210 220 230 240 KFLFVREPFE RLVSAYRNKF TQKYNISFHK RYGTKIIKRQ RKNATQEALR KGDDVKFEEF 250 260 270 280 290 300 VAYLIDPHTQ REEPFNEHWQ TVYSLCHPCH IHYDLVGKYE TLEEDSNYVL QLAGVGSYLK 310 320 330 340 350 FPTYAKSTRT TDEMTTEFFQ NISSEHQTQL YEVYKLDFLM FNYSVPSYLK LE
	Isoform 2 (C4S-1A) [UniParc]. Checksum: DEB2646BC0CA5FF8	FASTA	347	41,003
	10 20 30 40 50 60 MKPALLEVMR MNRICRMVLA TCLGSFILVI FYFQIMRRNP FGVDICCRKG SRSPLQELYN 70 80 90 100 110 120 PIQLELSNTA VLHQMRRDQV TDTCRANSAT SRKRRVLTPN DLKHLVVDED HELIYCYVPK 130 140 150 160 170 180 VACTNWKRLM MVLTGRGKYS DPMEIPANEA HVSANLKTLN QYSIPEINHR LKSYMKFLFV 190 200 210 220 230 240 REPFERLVSA YRNKFTQKYN ISFHKRYGTK IIKRQRKNAT QEALRKGDDV KFEEFVAYLI 250 260 270 280 290 300 DPHTQREEPF NEHWQTVYSL CHPCHIHYDL VGKYETLEED SNYVLQLAGV GSYLKFPTYA 310 320 330 340 KSTRTTDEMT TEFFQNISSE HQTQLYEVYK LDFLMFNYSV PSYLKLE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, expression, and chromosomal mapping of human chondroitin 4-sulfotransferase, whose expression pattern in human tissues is different from that of chondroitin 6-sulfotransferase." Okuda T., Mita S., Yamauchi S., Matsubara T., Yagi F., Yamamori D., Fukuta M., Kuroiwa A., Matsuda Y., Habuchi O. J. Biochem. 128:763-770(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, TISSUE SPECIFICITY. Tissue: Fetal brain.
[2]	"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] (ISOFORM 1), ENZYME ACTIVITY, TISSUE SPECIFICITY.
[3]	"Cloning and expression of a human chondroitin-4-sulfotransferase similar to members of the HNK-1 sulfotransferase family." Xia G., Evers M.R., Schachner M. Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[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] (ISOFORM 1).
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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] (ISOFORM 1). Tissue: Lung.
[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.
[8]	"Deregulation of the carbohydrate (chondroitin 4) sulfotransferase 11 (CHST11) gene in a B-cell chronic lymphocytic leukemia with a t(12;14)(q23;q32)." Schmidt H.H., Dyomin V.G., Palanisamy N., Itoyama T., Nanjangud G., Pirc-Danoewinata H., Haas O.A., Chaganti R.S.K. Oncogene 23:6991-6996(2004) [PubMed] [Europe PMC] [Abstract] Cited for: DISEASE, CHROMOSOMAL TRANSLOCATION WITH IGH.
[9]	"N-linked oligosaccharides are required to produce and stabilize the active form of chondroitin 4-sulphotransferase-1." Yusa A., Kitajima K., Habuchi O. Biochem. J. 388:115-121(2005) [PubMed] [Europe PMC] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION, MUTAGENESIS OF LYS-125; ASN-205; ASN-223 AND ASN-342.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB042326 mRNA. Translation: BAA95485.1. AF239820 mRNA. Translation: AAF81691.1. AJ269537 mRNA. Translation: CAB87380.1. AJ289134 mRNA. Translation: CAB92134.1. AK290923 mRNA. Translation: BAF83612.1. CH471054 Genomic DNA. Translation: EAW97748.1. BC013315 mRNA. Translation: AAH13315.1.
IPI	IPI00099831. IPI00554485.
PIR	JC7525.
RefSeq	NP_001167453.1. NM_001173982.1. NP_060883.1. NM_018413.5.
UniGene	Hs.17569.
3D structure databases
ProteinModelPortal	Q9NPF2.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000305725.
PTM databases
PhosphoSite	Q9NPF2.
Polymorphism databases
DMDM	61212137.
Proteomic databases
PaxDb	Q9NPF2.
PRIDE	Q9NPF2.
Protocols and materials databases
DNASU	50515.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000303694; ENSP00000305725; ENSG00000171310. ENST00000549260; ENSP00000450004; ENSG00000171310.
GeneID	50515.
KEGG	hsa:50515.
UCSC	uc001tky.3. human. uc001tkz.3. human.
Organism-specific databases
CTD	50515.
GeneCards	GC12P104783.
HGNC	HGNC:17422. CHST11.
HPA	HPA052828.
MIM	610128. gene.
neXtProt	NX_Q9NPF2.
PharmGKB	PA134875681.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG296625.
HOGENOM	HOG000231801.
HOVERGEN	HBG050952.
InParanoid	Q9NPF2.
KO	K01017.
OMA	TCRANSV.
OrthoDB	EOG4H19VW.
PhylomeDB	Q9NPF2.
Enzyme and pathway databases
BioCyc	MetaCyc:HS10284-MONOMER.
BRENDA	2.8.2.5. 2681.
Reactome	REACT_111217. Metabolism. REACT_116125. Disease.
Gene expression databases
ArrayExpress	Q9NPF2.
Bgee	Q9NPF2.
CleanEx	HS_CHST11.
Genevestigator	Q9NPF2.
Family and domain databases
InterPro	IPR018011. Carb_sulfotransferase-rel. IPR005331. Sulfotransferase. [Graphical view]
PANTHER	PTHR12137. PTHR12137. 1 hit.
Pfam	PF03567. Sulfotransfer_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CHST11. human.
GenomeRNAi	50515.
NextBio	53094.
SOURCE	Search...

Entry information

Entry name

CHSTB_HUMAN

Accession

Primary (citable) accession number: Q9NPF2
Secondary accession number(s): A8K4F8, Q9NXY6, Q9NY36

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.