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Q7L1S5 (CHST9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length443 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processCarbohydrate metabolism
   Cellular componentGolgi apparatus
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   Molecular functionTransferase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate 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

chondroitin sulfate metabolic process

Traceable author statement. Source: Reactome

glycosaminoglycan metabolic process

Non-traceable author statement Ref.2. Source: UniProtKB

hormone biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

proteoglycan biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

sulfur compound metabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentGolgi membrane

Traceable author statement. Source: Reactome

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Non-traceable author statement Ref.2. Source: UniProtKB

   Molecular_functionN-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 443443Carbohydrate sulfotransferase 9
PRO_0000189655

Regions

Topological domain1 – 1212Cytoplasmic Potential
Transmembrane13 – 3321Helical; Signal-anchor for type II membrane protein; Potential
Topological domain34 – 443410Lumenal Potential
Nucleotide binding220 – 2267PAPS By similarity
Nucleotide binding280 – 2889PAPS By similarity

Amino acid modifications

Glycosylation1591N-linked (GlcNAc...) Potential
Glycosylation2431N-linked (GlcNAc...) Potential
Glycosylation3241N-linked (GlcNAc...) Potential
Glycosylation4371N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence68 – 747MSTEKIQ → KPQVSHA in isoform 2.
VSP_043865
Alternative sequence75 – 443369Missing in isoform 2.
VSP_043866
Natural variant1221S → N.
Corresponds to variant rs17694469 [ dbSNP | Ensembl ].
VAR_055150

Experimental info

Sequence conflict1361R → H in AAK01862. Ref.1
Sequence conflict1501N → D in AAK01862. Ref.1
Sequence conflict194 – 1952HH → PP in AAK30370. Ref.2
Sequence conflict4421F → L in AAQ88852. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 5, 2009. Version 2.
Checksum: 5455E67D20C9F8D6

FASTA44352,055
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 1F1A2CBAD277FA16
Show »

FASTA748,591

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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.
CCDSCCDS42422.1. [Q7L1S5-1]
CCDS58618.1. [Q7L1S5-2]
RefSeqNP_001243245.1. NM_001256316.1. [Q7L1S5-2]
NP_113610.2. NM_031422.5. [Q7L1S5-1]
UniGeneHs.44584.
Hs.706552.

3D structure databases

ProteinModelPortalQ7L1S5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000392091.

PTM databases

PhosphoSiteQ7L1S5.

Polymorphism databases

DMDM229462829.

Proteomic databases

PaxDbQ7L1S5.
PRIDEQ7L1S5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000284224; ENSP00000284224; ENSG00000154080. [Q7L1S5-1]
ENST00000580774; ENSP00000464655; ENSG00000154080. [Q7L1S5-2]
ENST00000581714; ENSP00000462852; ENSG00000154080. [Q7L1S5-1]
GeneID83539.
KEGGhsa:83539.
UCSCuc002kwd.4. human. [Q7L1S5-1]
uc021uij.2. human. [Q7L1S5-2]

Organism-specific databases

CTD83539.
GeneCardsGC18M024495.
HGNCHGNC:19898. CHST9.
HPAHPA011393.
MIM610191. gene.
neXtProtNX_Q7L1S5.
PharmGKBPA134888782.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG296625.
HOGENOMHOG000231801.
HOVERGENHBG050950.
InParanoidQ7L1S5.
KOK09673.
OMANAQVVRQ.
OrthoDBEOG7B05D8.
PhylomeDBQ7L1S5.
TreeFamTF325581.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

BgeeQ7L1S5.
CleanExHS_CHST9.
GenevestigatorQ7L1S5.

Family and domain databases

InterProIPR018011. Carb_sulfotransferase-rel.
IPR005331. Sulfotransferase.
[Graphical view]
PANTHERPTHR12137. PTHR12137. 1 hit.
PfamPF03567. Sulfotransfer_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi83539.
NextBio72449.
PROQ7L1S5.
SOURCESearch...

Entry information

Entry nameCHST9_HUMAN
AccessionPrimary (citable) accession number: Q7L1S5
Secondary accession number(s): Q6UX69 expand/collapse secondary AC list , Q9BXH3, Q9BXH4, Q9BZW9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: May 5, 2009
Last modified: July 9, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM