Q7L1S5 (CHST9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Carbohydrate sulfotransferase 9
EC=2.8.2.-

Alternative name(s):
GalNAc-4-O-sulfotransferase 2
Short name=GalNAc-4-ST2
Short name=GalNAc4ST-2
N-acetylgalactosamine-4-O-sulfotransferase 2

Gene names

Name:	CHST9
ORF Names:	UNQ2549/PRO6175

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	443 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the transfer of sulfate to position 4 of non-reducing N-acetylgalactosamine (GalNAc) residues in both N-glycans and O-glycans. Participates in biosynthesis of glycoprotein hormones lutropin and thyrotropin, by mediating sulfation of their carbohydrate structures. Has a higher activity toward carbonic anhydrase VI than toward lutropin. Only active against terminal GalNAcbeta1,GalNAcbeta. Isoform 2, but not isoform 1, is active toward chondroitin.
Subcellular location	Isoform 1: Golgi apparatus membrane; Single-pass type II membrane protein By similarity. Isoform 2: Secreted Probable.
Tissue specificity	Highly expressed in trachea. Also expressed in fetal lung, adult pancreas, testis and salivary gland. Expressed at low level in pituitary gland, apex of the heart, adult lung, prostate and mammary gland. Weakly or not expressed in heart, liver and spinal cord. Ref.1 Ref.2
Sequence similarities	Belongs to the sulfotransferase 2 family.
Caution	It is uncertain whether Met-1 or Met-8 is the initiator.
Sequence caution	The sequence AAH25764.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAK01862.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAK30370.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Golgi apparatus Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
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 chondroitin sulfate biosynthetic process Traceable author statement. Source: Reactome hormone biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	Golgi membrane Traceable author statement. Source: Reactome extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Non-traceable author statement Ref.2. Source: UniProtKB
Molecular_function	N-acetylgalactosamine 4-O-sulfotransferase activity Inferred from direct assay Ref.2Ref.1. Source: UniProtKB
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q7L1S5-1)

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: Q7L1S5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     68-74: MSTEKIQ → KPQVSHA
     75-443: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 443	443	Carbohydrate sulfotransferase 9		PRO_0000189655
Regions
	Topological domain	1 – 12	12	Cytoplasmic Potential
	Transmembrane	13 – 33	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	34 – 443	410	Lumenal Potential
	Nucleotide binding	220 – 226	7	PAPS By similarity
	Nucleotide binding	280 – 288	9	PAPS By similarity
Amino acid modifications
	Glycosylation	159	1	N-linked (GlcNAc...) Potential
	Glycosylation	243	1	N-linked (GlcNAc...) Potential
	Glycosylation	324	1	N-linked (GlcNAc...) Potential
	Glycosylation	437	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	68 – 74	7	MSTEKIQ → KPQVSHA in isoform 2.		VSP_043865
	Alternative sequence	75 – 443	369	Missing in isoform 2.		VSP_043866
	Natural variant	122	1	S → N. Corresponds to variant rs17694469 [ dbSNP | Ensembl ].		VAR_055150
Experimental info
	Sequence conflict	136	1	R → H in AAK01862. Ref.1
	Sequence conflict	150	1	N → D in AAK01862. Ref.1
	Sequence conflict	194 – 195	2	HH → PP in AAK30370. Ref.2
	Sequence conflict	442	1	F → L in AAQ88852. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 5, 2009. Version 2. Checksum: 5455E67D20C9F8D6	FASTA	443	52,055
	10 20 30 40 50 60 MQPSEMVMNP KQVFLSVLIF GVAGLLLFMY LQVWIEEQHT GRVEKRREQK VTSGWGPVKY 70 80 90 100 110 120 LRPVPRIMST EKIQEHITNQ NPKFHMPEDV REKKENLLLN SERSTRLLTK TSHSQGGDQA 130 140 150 160 170 180 LSKSTGSPTE KLIEKRQGAK TVFNKFSNMN WPVDIHPLNK SLVKDNKWKK TEETQEKRRS 190 200 210 220 230 240 FLQEFCKKYG GVSHHQSHLF HTVSRIYVED KHKILYCEVP KAGCSNWKRI LMVLNGLASS 250 260 270 280 290 300 AYNISHNAVH YGKHLKKLDS FDLKGIYTRL NTYTKAVFVR DPMERLVSAF RDKFEHPNSY 310 320 330 340 350 360 YHPVFGKAII KKYRPNACEE ALINGSGVKF KEFIHYLLDS HRPVGMDIHW EKVSKLCYPC 370 380 390 400 410 420 LINYDFVGKF ETLEEDANYF LQMIGAPKEL KFPNFKDRHS SDERTNAQVV RQYLKDLTRT 430 440 ERQLIYDFYY LDYLMFNYTT PFL
	Isoform 2 [UniParc]. Checksum: 1F1A2CBAD277FA16	FASTA	74	8,591
	10 20 30 40 50 60 MQPSEMVMNP KQVFLSVLIF GVAGLLLFMY LQVWIEEQHT GRVEKRREQK VTSGWGPVKY 70 LRPVPRIKPQ VSHA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and expression of two distinct human N-acetylgalactosamine 4-O-sulfotransferases that transfer sulfate to GalNAc beta 1->4GlcNAc beta 1->R in both N- and O-glycans." Hiraoka N., Misra A., Belot F., Hindsgaul O., Fukuda M. Glycobiology 11:495-504(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, TISSUE SPECIFICITY.
[2]	"Molecular cloning and expression of an N-acetylgalactosamine-4-O-sulfotransferase that transfers sulfate to terminal and non-terminal beta 1,4-linked N-acetylgalactosamine." Kang H.-G., Evers M.R., Xia G., Baenziger J.U., Schachner M. J. Biol. Chem. 276:10861-10869(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ENZYME ACTIVITY, TISSUE SPECIFICITY.
[3]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[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). Tissue: Testis.
[5]	"DNA sequence and analysis of human chromosome 18." Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S. Nature 437:551-555(2005) [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] (ISOFORM 1). Tissue: Lung.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF239821 mRNA. Translation: AAK01862.1. Different initiation. AF332472 mRNA. Translation: AAK30369.1. AF332473 mRNA. Translation: AAK30370.1. Sequence problems. AY358488 mRNA. Translation: AAQ88852.1. AK093349 mRNA. Translation: BAC04141.1. AC010854 Genomic DNA. No translation available. AC023575 Genomic DNA. No translation available. AC116017 Genomic DNA. No translation available. BC025764 mRNA. Translation: AAH25764.2. Different initiation.
IPI	IPI00000111. IPI00554505.
RefSeq	NP_001243245.1. NM_001256316.1. NP_113610.2. NM_031422.5.
UniGene	Hs.44584. Hs.706552.
3D structure databases
ProteinModelPortal	Q7L1S5.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000392091.
PTM databases
PhosphoSite	Q7L1S5.
Polymorphism databases
DMDM	229462829.
Proteomic databases
PaxDb	Q7L1S5.
PRIDE	Q7L1S5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000284224; ENSP00000284224; ENSG00000154080. ENST00000580774; ENSP00000464655; ENSG00000154080. ENST00000581714; ENSP00000462852; ENSG00000154080.
GeneID	83539.
KEGG	hsa:83539.
UCSC	uc002kwd.3. human.
Organism-specific databases
CTD	83539.
GeneCards	GC18M024495.
HGNC	HGNC:19898. CHST9.
HPA	HPA011393.
MIM	610191. gene.
neXtProt	NX_Q7L1S5.
PharmGKB	PA134888782.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG296625.
HOGENOM	HOG000231801.
HOVERGEN	HBG050950.
InParanoid	Q7L1S5.
KO	K09673.
OMA	NAQVVRQ.
OrthoDB	EOG4RJG1F.
PhylomeDB	Q7L1S5.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism. REACT_116125. Disease.
Gene expression databases
Bgee	Q7L1S5.
CleanEx	HS_CHST9.
Genevestigator	Q7L1S5.
GermOnline	ENSG00000154080. Homo sapiens.
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
GenomeRNAi	83539.
NextBio	72449.
SOURCE	Search...

Entry information

Entry name

CHST9_HUMAN

Accession

Primary (citable) accession number: Q7L1S5
Secondary accession number(s): Q6UX69 , Q9BXH3, Q9BXH4, Q9BZW9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	May 5, 2009
Last modified:	April 3, 2013
This is version 85 of the entry and version 2 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.