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Q8N6G5 (CGAT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Protein attributes

Sequence length542 AA.
Sequence statusComplete.
Protein existenceEvidence 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 apparatusGolgi 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 componentGolgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Signal-anchor
Transmembrane
Transmembrane helix
   LigandMetal-binding
   Molecular functionTransferase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate 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

chondroitin sulfate proteoglycan biosynthetic process

Inferred from direct assay PubMed 11788602. Source: UniProtKB

chondroitin sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process

Traceable author statement PubMed 11788602. Source: UniProtKB

dermatan sulfate proteoglycan biosynthetic process

Inferred from direct assay PubMed 11788602. Source: UniProtKB

dermatan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process

Traceable author statement PubMed 11788602. Source: UniProtKB

glycosaminoglycan metabolic process

Traceable author statement. Source: Reactome

proteoglycan biosynthetic process

Inferred from direct assay PubMed 11788602. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi cisterna membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Golgi membrane

Traceable author statement. Source: Reactome

integral component of Golgi membrane

Non-traceable author statement PubMed 11788602. Source: UniProtKB

   Molecular_functionacetylgalactosaminyltransferase activity

Inferred from direct assay PubMed 11788602. Source: UniProtKB

glucuronylgalactosylproteoglycan 4-beta-N-acetylgalactosaminyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 542542Chondroitin sulfate N-acetylgalactosaminyltransferase 2
PRO_0000189566

Regions

Topological domain1 – 1111Cytoplasmic Potential
Transmembrane12 – 3221Helical; Signal-anchor for type II membrane protein; Potential
Topological domain33 – 542510Lumenal Potential
Coiled coil59 – 10547 Potential

Sites

Metal binding3691Divalent metal cation Potential
Metal binding4861Divalent metal cation Potential

Amino acid modifications

Glycosylation411N-linked (GlcNAc...) Potential
Glycosylation3331N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence327 – 3337SESNFHN → RLASSTW in isoform 2.
VSP_012729
Alternative sequence334 – 542209Missing in isoform 2.
VSP_012730
Natural variant2151E → K.
Corresponds to variant rs11238456 [ dbSNP | Ensembl ].
VAR_048715
Natural variant4791P → S. Ref.4
Corresponds to variant rs2435381 [ dbSNP | Ensembl ].
VAR_048716

Experimental info

Sequence conflict4381Y → H in BAB85092. Ref.3

Sequences

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

Last modified October 1, 2002. Version 1.
Checksum: E19103EE6F903AB6

FASTA54262,572
        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 

« Hide

Isoform 2 [UniParc].

Checksum: C802C5BB271F54FB
Show »

FASTA33338,440

References

« Hide '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. 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: 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. expand/collapse author list , 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.
RefSeqNP_061060.3. NM_018590.4.
XP_005271877.1. XM_005271820.2.
UniGeneHs.657569.
Hs.744559.

3D structure databases

ProteinModelPortalQ8N6G5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000363590.

Protein family/group databases

CAZyGT7. Glycosyltransferase Family 7.

Polymorphism databases

DMDM60391915.

Proteomic databases

PaxDbQ8N6G5.
PRIDEQ8N6G5.

Protocols and materials databases

DNASU55454.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374464; ENSP00000363588; ENSG00000169826. [Q8N6G5-2]
ENST00000374466; ENSP00000363590; ENSG00000169826. [Q8N6G5-1]
GeneID55454.
KEGGhsa:55454.
UCSCuc001jam.2. human. [Q8N6G5-2]
uc001jan.4. human. [Q8N6G5-1]

Organism-specific databases

CTD55454.
GeneCardsGC10P043633.
HGNCHGNC:24292. CSGALNACT2.
HPAHPA031539.
HPA031540.
neXtProtNX_Q8N6G5.
PharmGKBPA162382854.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG295515.
HOGENOMHOG000294238.
HOVERGENHBG050930.
InParanoidQ8N6G5.
KOK00746.
OMANVGARAW.
OrthoDBEOG75TMBN.
PhylomeDBQ8N6G5.
TreeFamTF318303.

Enzyme and pathway databases

BioCycMetaCyc:HS10013-MONOMER.
BRENDA2.4.1.174. 2681.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

BgeeQ8N6G5.
CleanExHS_CSGALNACT2.
GenevestigatorQ8N6G5.

Family and domain databases

InterProIPR008428. Chond_GalNAc.
[Graphical view]
PANTHERPTHR12369. PTHR12369. 1 hit.
PfamPF05679. CHGN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCSGALNACT2. human.
GenomeRNAi55454.
NextBio59849.
PROQ8N6G5.

Entry information

Entry nameCGAT2_HUMAN
AccessionPrimary (citable) accession number: Q8N6G5
Secondary accession number(s): B3KWL7 expand/collapse secondary AC list , Q6MZJ5, Q6MZP6, Q8TCH4, Q9P1I6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 110 of the entry and version 1 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

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 10

Human chromosome 10: entries, gene names and cross-references to MIM