Reviewed, UniProtKB/Swiss-Prot Q8IZ52 (CHSS2_HUMAN)

Names and origin

Protein names

Recommended name:
    Chondroitin sulfate synthase 2
    EC=2.4.1.175
Alternative name(s):
    Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase II
    N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase II
    EC=2.4.1.226
    Chondroitin glucuronyltransferase II
    N-acetylgalactosaminyltransferase
    Chondroitin-polymerizing factor

Gene names

Name:	CHPF
Synonyms:	CSS2
ORF Names:	UNQ651/PRO1281

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	775 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.2
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 manganese. Can also utilize cobalt. Ref.2
Subunit structure	Binds CHSY1.
Subcellular location	Golgi apparatus › Golgi stack membrane; Single-pass type II membrane protein Probable.
Tissue specificity	Ubiquitous. Highly expressed in pancreas, ovary, brain, heart, skeletal muscle, colon, kidney, liver, stomach, small intestine and placenta. Ref.2 Ref.1
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.8
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 Phosphoprotein
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 protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EXOSC10	Q01780	1	EBI-372500,EBI-358236

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 775	775	Chondroitin sulfate synthase 2		PRO_0000189560
Regions
	Topological domain	1 – 15	15	Cytoplasmic Potential
	Transmembrane	16 – 34	19	Signal-anchor for type II membrane protein Potential
	Topological domain	35 – 775	741	Lumenal Potential
	Compositional bias	515 – 571	57	Ala-rich
Sites
	Metal binding	617	1	Divalent metal cation Potential
Amino acid modifications
	Modified residue	126	1	Phosphoserine Ref.8
	Modified residue	129	1	Phosphothreonine Ref.8
	Glycosylation	138	1	N-linked (GlcNAc...) Potential
	Glycosylation	361	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	371	1	R → Q: dbSNP rs6436155. Ref.4		VAR_047394
Experimental info
	Sequence conflict	650	1	A → G in AAQ88769. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q8IZ52-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 78FE2615617539C2	FASTA	775	85,495
	10 20 30 40 50 60 MRASLLLSVL RPAGPVAVGI SLGFTLSLLS VTWVEEPCGP GPPQPGDSEL PPRGNTNAAR 70 80 90 100 110 120 RPNSVQPGAE REKPGAGEGA GENWEPRVLP YHPAQPGQAA KKAVRTRYIS TELGIRQRLL 130 140 150 160 170 180 VAVLTSQTTL PTLGVAVNRT LGHRLERVVF LTGARGRRAP PGMAVVTLGE ERPIGHLHLA 190 200 210 220 230 240 LRHLLEQHGD DFDWFFLVPD TTYTEAHGLA RLTGHLSLAS AAHLYLGRPQ DFIGGEPTPG 250 260 270 280 290 300 RYCHGGFGVL LSRMLLQQLR PHLEGCRNDI VSARPDEWLG RCILDATGVG CTGDHEGVHY 310 320 330 340 350 360 SHLELSPGEP VQEGDPHFRS ALTAHPVRDP VHMYQLHKAF ARAELERTYQ EIQELQWEIQ 370 380 390 400 410 420 NTSHLAVDGD RAAAWPVGIP APSRPASRFE VLRWDYFTEQ HAFSCADGSP RCPLRGADRA 430 440 450 460 470 480 DVADVLGTAL EELNRRYHPA LRLQKQQLVN GYRRFDPARG MEYTLDLQLE ALTPQGGRRP 490 500 510 520 530 540 LTRRVQLLRP LSRVEILPVP YVTEASRLTV LLPLAAAERD LAPGFLEAFA TAALEPGDAA 550 560 570 580 590 600 AALTLLLLYE PRQAQRVAHA DVFAPVKAHV AELERRFPGA RVPWLSVQTA APSPLRLMDL 610 620 630 640 650 660 LSKKHPLDTL FLLAGPDTVL TPDFLNRCRM HAISGWQAFF PMHFQAFHPA VAPPQGPGPP 670 680 690 700 710 720 ELGRDTGRFD RQAASEACFY NSDYVAARGR LAAASEQEEE LLESLDVYEL FLHFSSLHVL 730 740 750 760 770 RAVEPALLQR YRAQTCSARL SEDLYHRCLQ SVLEGLGSRT QLAMLLFEQE QGNST

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CHSY1, TISSUE SPECIFICITY.
[2]	"Chondroitin sulfate synthase-2. Molecular cloning and characterization of a novel human glycosyltransferase homologous to chondroitin sulfate glucuronyltransferase, which has dual enzymatic activities." Yada T., Gotoh M., Sato T., Shionyu M., Go M., Kaseyama H., Iwasaki H., Kikuchi N., Kwon Y.-D., Togayachi A., Kudo T., Watanabe H., Narimatsu H., Kimata K. J. Biol. Chem. 278:30235-30247(2003) [PubMed: 12761225] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, COFACTOR, 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: 12975309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLN-371.
[5]	"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, Muscle and Skin.
[6]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 210-775. Tissue: Testis.
[7]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 451-775. Tissue: Small intestine.
[8]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126 AND THR-129, MASS SPECTROMETRY.

Web resources

GGDB

GlycoGene database

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB095813 mRNA. Translation: BAC78393.1. AB086063 mRNA. Translation: BAC81536.1. AY358403 mRNA. Translation: AAQ88769.1. AC009955 Genomic DNA. No translation available. BC008878 mRNA. Translation: AAH08878.2. BC021223 mRNA. Translation: AAH21223.2. BC023531 mRNA. Translation: AAH23531.1. AL136814 mRNA. Translation: CAB66748.2. AK026331 mRNA. Translation: BAB15449.1. Different initiation.
IPI	IPI00465319.
RefSeq	NP_078812.2.
UniGene	Hs.516711
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8IZ52. 2 interactions.
Protein family/group databases
CAZy	GT31. Glycosyltransferase Family 31. GT7. Glycosyltransferase Family 7.
PTM databases
PhosphoSite	Q8IZ52.
Proteomic databases
PRIDE	Q8IZ52.
Genome annotation databases
Ensembl	ENSG00000123989. Homo sapiens. [Contig view]
GeneID	79586.
KEGG	hsa:79586.
UCSC	uc002vmc.2. human.
Organism-specific databases
GeneCards	GC02M220111.
H-InvDB	HIX0002868.
HGNC	HGNC:24291. CHPF.
MIM	610405. gene.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q8IZ52.
HOVERGEN	Q8IZ52.
Enzyme and pathway databases
BRENDA	2.4.1.175. 247. 2.4.1.226. 247.
Gene expression databases
ArrayExpress	Q8IZ52.
Bgee	Q8IZ52.
CleanEx	HS_CHPF.
GermOnline	ENSG00000123989. 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	68587.
SOURCE	Search...

Entry information

Entry name

CHSS2_HUMAN

Accession

Primary (citable) accession number: Q8IZ52
Secondary accession number(s): Q6UXD6 , Q7L4G1, Q9H0F8, Q9H618

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	March 1, 2003
Last modified:	July 7, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)