Q8N6G5 (CGAT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chondroitin sulfate N-acetylgalactosaminyltransferase 2
EC=2.4.1.174

Alternative name(s):
Chondroitin beta-1,4-N-acetylgalactosaminyltransferase 2
Short name=Beta4GalNAcT-2
Short name=GalNAcT-2

Gene names

Name:	CSGALNACT2
Synonyms:	CHGN2, GALNACT2
ORF Names:	PRO0082

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

General annotation (Comments)

Function	Transfers 1,4-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of glucuronic acid (GlcUA). Required for addition of the first GalNAc to the core tetrasaccharide linker and for elongation of chondroitin chains. Ref.1 Ref.2
Catalytic activity	UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan = UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan.
Subcellular location	Golgi apparatus › Golgi stack membrane; Single-pass type II membrane protein Probable.
Tissue specificity	Ubiquitous. Ref.1 Ref.2
Sequence similarities	Belongs to the chondroitin N-acetylgalactosaminyltransferase family.
Sequence caution	The sequence AAF71068.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Signal-anchor Transmembrane Transmembrane helix
Ligand	Metal-binding
Molecular function	Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chondroitin sulfate biosynthetic process Traceable author statement. Source: Reactome chondroitin sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process Traceable author statement PubMed 11788602. Source: UniProtKB dermatan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process Traceable author statement PubMed 11788602. Source: UniProtKB
Cellular_component	Golgi cisterna membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to Golgi membrane Non-traceable author statement PubMed 11788602. Source: UniProtKB
Molecular_function	acetylgalactosaminyltransferase activity Inferred from direct assay PubMed 11788602. Source: UniProtKB glucuronylgalactosylproteoglycan 4-beta-N-acetylgalactosaminyltransferase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q8N6G5-1)

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: Q8N6G5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     327-333: SESNFHN → RLASSTW
     334-542: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 542	542	Chondroitin sulfate N-acetylgalactosaminyltransferase 2		PRO_0000189566
Regions
	Topological domain	1 – 11	11	Cytoplasmic Potential
	Transmembrane	12 – 32	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	33 – 542	510	Lumenal Potential
	Coiled coil	59 – 105	47	Potential
Sites
	Metal binding	369	1	Divalent metal cation Potential
	Metal binding	486	1	Divalent metal cation Potential
Amino acid modifications
	Glycosylation	41	1	N-linked (GlcNAc...) Potential
	Glycosylation	333	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	327 – 333	7	SESNFHN → RLASSTW in isoform 2.		VSP_012729
	Alternative sequence	334 – 542	209	Missing in isoform 2.		VSP_012730
	Natural variant	215	1	E → K. Corresponds to variant rs11238456 [ dbSNP | Ensembl ].		VAR_048715
	Natural variant	479	1	P → S. Ref.4 Corresponds to variant rs2435381 [ dbSNP | Ensembl ].		VAR_048716
Experimental info
	Sequence conflict	438	1	Y → H in BAB85092. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: E19103EE6F903AB6	FASTA	542	62,572
	10 20 30 40 50 60 MPRRGLILHT RTHWLLLGLA LLCSLVLFMY LLECAPQTDG NASLPGVVGE NYGKEYYQAL 70 80 90 100 110 120 LQEQEEHYQT RATSLKRQIA QLKQELQEMS EKMRSLQERR NVGANGIGYQ SNKEQAPSDL 130 140 150 160 170 180 LEFLHSQIDK AEVSIGAKLP SEYGVIPFES FTLMKVFQLE MGLTRHPEEK PVRKDKRDEL 190 200 210 220 230 240 VEVIEAGLEV INNPDEDDEQ EDEEGPLGEK LIFNENDFVE GYYRTERDKG TQYELFFKKA 250 260 270 280 290 300 DLTEYRHVTL FRPFGPLMKV KSEMIDITRS IINIIVPLAE RTEAFVQFMQ NFRDVCIHQD 310 320 330 340 350 360 KKIHLTVVYF GKEGLSKVKS ILESVTSESN FHNYTLVSLN EEFNRGRGLN VGARAWDKGE 370 380 390 400 410 420 VLMFFCDVDI YFSAEFLNSC RLNAEPGKKV FYPVVFSLYN PAIVYANQEV PPPVEQQLVH 430 440 450 460 470 480 KKDSGFWRDF GFGMTCQYRS DFLTIGGFDM EVKGWGGEDV HLYRKYLHGD LIVIRTPVPG 490 500 510 520 530 540 LFHLWHEKRC ADELTPEQYR MCIQSKAMNE ASHSHLGMLV FREEIETHLH KQAYRTNSEA VG
	Isoform 2 [UniParc]. Checksum: C802C5BB271F54FB	FASTA	333	38,440
	10 20 30 40 50 60 MPRRGLILHT RTHWLLLGLA LLCSLVLFMY LLECAPQTDG NASLPGVVGE NYGKEYYQAL 70 80 90 100 110 120 LQEQEEHYQT RATSLKRQIA QLKQELQEMS EKMRSLQERR NVGANGIGYQ SNKEQAPSDL 130 140 150 160 170 180 LEFLHSQIDK AEVSIGAKLP SEYGVIPFES FTLMKVFQLE MGLTRHPEEK PVRKDKRDEL 190 200 210 220 230 240 VEVIEAGLEV INNPDEDDEQ EDEEGPLGEK LIFNENDFVE GYYRTERDKG TQYELFFKKA 250 260 270 280 290 300 DLTEYRHVTL FRPFGPLMKV KSEMIDITRS IINIIVPLAE RTEAFVQFMQ NFRDVCIHQD 310 320 330 KKIHLTVVYF GKEGLSKVKS ILESVTRLAS STW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Differential roles of two N-acetylgalactosaminyltransferases, CSGalNAcT-1, and a novel enzyme, CSGalNAcT-2. Initiation and elongation in synthesis of chondroitin sulfate." Sato T., Gotoh M., Kiyohara K., Akashima T., Iwasaki H., Kameyama A., Mochizuki H., Yada T., Inaba N., Togayachi A., Kudo T., Asada M., Watanabe H., Imamura T., Kimata K., Narimatsu H. J. Biol. Chem. 278:3063-3071(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
[2]	"Molecular cloning and expression of a second chondroitin N-acetylgalactosaminyltransferase involved in the initiation and elongation of chondroitin/dermatan sulfate." Uyama T., Kitagawa H., Tanaka J., Tamura J., Ogawa T., Sugahara K. J. Biol. Chem. 278:3072-3078(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
[3]	"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: Lung.
[4]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT SER-479. Tissue: Endothelial cell and Small intestine.
[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: Pancreas.
[7]	"Gene expression profiling in human fetal liver and identification of tissue- and developmental-stage-specific genes through compiled expression profiles and efficient cloning of full-length cDNAs." Yu Y., Zhang C., Zhou G., Wu S., Qu X., Wei H., Xing G., Dong C., Zhai Y., Wan J., Ouyang S., Li L., Zhang S., Zhou K., Zhang Y., Wu C., He F. Genome Res. 11:1392-1403(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 418-542 (ISOFORM 1). Tissue: Fetal liver.
+	Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Chondroitin beta-1,4-N-acetylgalactosaminyltransferase 2

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB079252 mRNA. Translation: BAC55935.1. AB090811 mRNA. Translation: BAC55936.1. AK074474 mRNA. Translation: BAB85092.1. AK125300 mRNA. Translation: BAG54179.1. BX640967 mRNA. Translation: CAE45982.1. BX641073 mRNA. Translation: CAE46036.1. CH471160 Genomic DNA. Translation: EAW86587.1. BC030268 mRNA. Translation: AAH30268.1. AF116646 mRNA. Translation: AAF71068.1. Different initiation.
IPI	IPI00171135. IPI00549699.
RefSeq	NP_061060.3. NM_018590.4.
UniGene	Hs.657569. Hs.744559.
3D structure databases
ProteinModelPortal	Q8N6G5.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000363590.
Protein family/group databases
CAZy	GT7. Glycosyltransferase Family 7.
Polymorphism databases
DMDM	60391915.
Proteomic databases
PaxDb	Q8N6G5.
PRIDE	Q8N6G5.
Protocols and materials databases
DNASU	55454.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000374464; ENSP00000363588; ENSG00000169826. ENST00000374466; ENSP00000363590; ENSG00000169826.
GeneID	55454.
KEGG	hsa:55454.
UCSC	uc001jam.1. human. uc001jan.3. human.
Organism-specific databases
CTD	55454.
GeneCards	GC10P043633.
HGNC	HGNC:24292. CSGALNACT2.
HPA	HPA031539. HPA031540.
neXtProt	NX_Q8N6G5.
PharmGKB	PA162382854.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG295515.
HOGENOM	HOG000294238.
HOVERGEN	HBG050930.
InParanoid	Q8N6G5.
KO	K00746.
OMA	FMQNFRD.
OrthoDB	EOG4J6RQR.
PhylomeDB	Q8N6G5.
Enzyme and pathway databases
BioCyc	MetaCyc:HS10013-MONOMER.
BRENDA	2.4.1.174. 2681.
Reactome	REACT_111217. Metabolism. REACT_116125. Disease.
Gene expression databases
Bgee	Q8N6G5.
CleanEx	HS_CSGALNACT2.
Genevestigator	Q8N6G5.
GermOnline	ENSG00000169826. Homo sapiens.
Family and domain databases
InterPro	IPR008428. Chond_GalNAc. [Graphical view]
PANTHER	PTHR12369. PTHR12369. 1 hit.
Pfam	PF05679. CHGN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CSGALNACT2. human.
GenomeRNAi	55454.
NextBio	59849.

Entry information

Entry name

CGAT2_HUMAN

Accession

Primary (citable) accession number: Q8N6G5
Secondary accession number(s): B3KWL7 , Q6MZJ5, Q6MZP6, Q8TCH4, Q9P1I6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	October 1, 2002
Last modified:	May 29, 2013
This is version 102 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.