Reviewed, UniProtKB/Swiss-Prot Q86X52 (CHSS1_HUMAN)

Names and origin

Protein names

Recommended name:
    Chondroitin sulfate synthase 1
    EC=2.4.1.175
Alternative name(s):
    Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase 1
    N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase 1
    EC=2.4.1.226
    Chondroitin glucuronyltransferase II
    N-acetylgalactosaminyltransferase II

Gene names

Name:	CHSY1
Synonyms:	CHSY, CSS1, KIAA0990
ORF Names:	UNQ756/PRO1487

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	802 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Has both beta-1,3-glucuronic acid and beta-1,4-N-acetylgalactosamine transferase activity. Transfers glucuronic acid (GlcUA) from UDP-GlcUA and N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of the elongating chondroitin polymer. Ref.1
Catalytic activity	UDP-N-acetyl-D-galactosamine + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-proteoglycan = UDP + N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-proteoglycan. UDP-alpha-D-glucuronate + N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan = UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan.
Cofactor	Divalent cations. Highest activities are measured with cobalt, manganese and cadmium. Ref.6
Subunit structure	Binds CHPF.
Subcellular location	Golgi apparatus › Golgi stack membrane; Single-pass type II membrane protein Probable.
Tissue specificity	Ubiquitous, with the highest levels in placenta. Detected at low levels in brain, heart, skeletal muscle, colon, thymus, spleen, kidney, liver, adrenal gland, mammary gland, stomach, small intestine, lung and peripheral blood leukocytes. Ref.1 Ref.6
Sequence similarities	Belongs to the chondroitin N-acetylgalactosaminyltransferase family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Polymorphism
Domain	Signal-anchor Transmembrane
Ligand	Metal-binding
Molecular function	Transferase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	Golgi cisterna membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase activity Inferred from electronic annotation. Source: EC glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 802	802	Chondroitin sulfate synthase 1		PRO_0000189558
Regions
	Topological domain	1 – 7	7	Cytoplasmic Potential
	Transmembrane	8 – 28	21	Signal-anchor for type II membrane protein Potential
	Topological domain	29 – 802	774	Lumenal Potential
	Compositional bias	449 – 454	6	Poly-Leu
Sites
	Metal binding	633	1	Divalent metal cation Potential
	Metal binding	747	1	Divalent metal cation Potential
Amino acid modifications
	Glycosylation	189	1	N-linked (GlcNAc...) Potential
	Glycosylation	623	1	N-linked (GlcNAc...) Potential
	Glycosylation	796	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	359	1	P → S: dbSNP rs3743193.		VAR_021173
	Natural variant	652	1	Q → H: dbSNP rs4426333.		VAR_028009
Experimental info
	Sequence conflict	274	1	Q → R in AAQ88893. Ref.2
	Sequence conflict	588	1	R → T Ref.1
	Sequence conflict	588	1	R → T Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q86X52-1 [UniParc]. Last modified October 17, 2006. Version 3. Checksum: 5B4C02670332FA0E	FASTA	802	91,784
	10 20 30 40 50 60 MAARGRRAWL SVLLGLVLGF VLASRLVLPR ASELKRAGPR RRASPEGCRS GQAAASQAGG 70 80 90 100 110 120 ARGDARGAQL WPPGSDPDGG PRDRNFLFVG VMTAQKYLQT RAVAAYRTWS KTIPGKVQFF 130 140 150 160 170 180 SSEGSDTSVP IPVVPLRGVD DSYPPQKKSF MMLKYMHDHY LDKYEWFMRA DDDVYIKGDR 190 200 210 220 230 240 LENFLRSLNS SEPLFLGQTG LGTTEEMGKL ALEPGENFCM GGPGVIMSRE VLRRMVPHIG 250 260 270 280 290 300 KCLREMYTTH EDVEVGRCVR RFAGVQCVWS YEMQQLFYEN YEQNKKGYIR DLHNSKIHQA 310 320 330 340 350 360 ITLHPNKNPP YQYRLHSYML SRKISELRHR TIQLHREIVL MSKYSNTEIH KEDLQLGIPP 370 380 390 400 410 420 SFMRFQPRQR EEILEWEFLT GKYLYSAVDG QPPRRGMDSA QREALDDIVM QVMEMINANA 430 440 450 460 470 480 KTRGRIIDFK EIQYGYRRVN PMYGAEYILD LLLLYKKHKG KKMTVPVRRH AYLQQTFSKI 490 500 510 520 530 540 QFVEHEELDA QELAKRINQE SGSLSFLSNS LKKLVPFQLP GSKSEHKEPK DKKINILIPL 550 560 570 580 590 600 SGRFDMFVRF MGNFEKTCLI PNQNVKLVVL LFNSDSNPDK AKQVELMRDY RIKYPKADMQ 610 620 630 640 650 660 ILPVSGEFSR ALALEVGSSQ FNNESLLFFC DVDLVFTTEF LQRCRANTVL GQQIYFPIIF 670 680 690 700 710 720 SQYDPKIVYS GKVPSDNHFA FTQKTGFWRN YGFGITCIYK GDLVRVGGFD VSIQGWGLED 730 740 750 760 770 780 VDLFNKVVQA GLKTFRSQEV GVVHVHHPVF CDPNLDPKQY KMCLGSKAST YGSTQQLAEM 790 800 WLEKNDPSYS KSSNNNGSVR TA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and expression of a human chondroitin synthase." Kitagawa H., Uyama T., Sugahara K. J. Biol. Chem. 276:38721-38726(2001) [PubMed: 11514575] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[2]	"Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 6:63-70(1999) [PubMed: 10231032] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[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: 12975309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[5]	"Molecular cloning of a chondroitin polymerizing factor that cooperates with chondroitin synthase for chondroitin polymerization." Kitagawa H., Izumikawa T., Uyama T., Sugahara K. J. Biol. Chem. 278:23666-23671(2003) [PubMed: 12716890] [Abstract] Cited for: INTERACTION WITH CHPF.
[6]	"Chondroitin sulfate synthase-3. Molecular cloning and characterization." Yada T., Sato T., Kaseyama H., Gotoh M., Iwasaki H., Kikuchi N., Kwon Y.-D., Togayachi A., Kudo T., Watanabe H., Narimatsu H., Kimata K. J. Biol. Chem. 278:39711-39725(2003) [PubMed: 12907687] [Abstract] Cited for: COFACTOR, TISSUE SPECIFICITY.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Chondroitin sulfate synthase 1

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB071402 mRNA. Translation: BAB64936.1. AB023207 mRNA. Translation: BAA76834.2. Different initiation. AY358529 mRNA. Translation: AAQ88893.1. BC046247 mRNA. Translation: AAH46247.1.
IPI	IPI00329141.
RefSeq	NP_055733.2.
UniGene	Hs.110488
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GT31. Glycosyltransferase Family 31. GT7. Glycosyltransferase Family 7.
PTM databases
PhosphoSite	Q86X52.
Proteomic databases
PRIDE	Q86X52.
Genome annotation databases
Ensembl	ENSG00000131873. Homo sapiens. [Contig view]
GeneID	22856.
KEGG	hsa:22856.
UCSC	uc002bwt.1. human.
Organism-specific databases
GeneCards	GC15M099533.
H-InvDB	HIX0012628.
HGNC	HGNC:17198. CHSY1.
MIM	608183. gene.
PharmGKB	PA26509.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q86X52.
HOVERGEN	Q86X52.
OMA	Q86X52. INANAKT.
Enzyme and pathway databases
BRENDA	2.4.1.175. 247. 2.4.1.226. 247.
Gene expression databases
ArrayExpress	Q86X52.
Bgee	Q86X52.
CleanEx	HS_CHSY1.
GermOnline	ENSG00000131873. Homo sapiens.
Family and domain databases
InterPro	IPR008428. Chond_GalNAc. [Graphical view]
PANTHER	PTHR12369. CHGN. 1 hit.
Pfam	PF05679. CHGN. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	43341.
SOURCE	Search...

Entry information

Entry name

CHSS1_HUMAN

Accession

Primary (citable) accession number: Q86X52
Secondary accession number(s): Q6UX38, Q7LFU5, Q9Y2J5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	October 17, 2006
Last modified:	July 7, 2009
This is version 58 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)