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Protein

Chondroitin sulfate N-acetylgalactosaminyltransferase 2

Gene

Csgalnact2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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 (By similarity).By similarity

Catalytic activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi369 – 3691Divalent metal cationSequence analysis
Metal bindingi486 – 4861Divalent metal cationSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-2022870. Chondroitin sulfate biosynthesis.

Protein family/group databases

CAZyiGT7. Glycosyltransferase Family 7.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Csgalnact2
Synonyms:Chgn2, Galnact2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1926002. Csgalnact2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1313CytoplasmicSequence analysisAdd
BLAST
Transmembranei14 – 3421Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini35 – 542508LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 542542Chondroitin sulfate N-acetylgalactosaminyltransferase 2PRO_0000189567Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi41 – 411N-linked (GlcNAc...)Sequence analysis
Glycosylationi333 – 3331N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiQ8C1F4.
MaxQBiQ8C1F4.
PaxDbiQ8C1F4.
PRIDEiQ8C1F4.

Expressioni

Gene expression databases

BgeeiQ8C1F4.
ExpressionAtlasiQ8C1F4. baseline and differential.
GenevisibleiQ8C1F4. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000039819.

Structurei

3D structure databases

ProteinModelPortaliQ8C1F4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili59 – 10547Sequence analysisAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3588. Eukaryota.
ENOG410XNYM. LUCA.
GeneTreeiENSGT00760000119143.
HOGENOMiHOG000230628.
HOVERGENiHBG050930.
InParanoidiQ8C1F4.
KOiK00746.
OMAiNVGARAW.
OrthoDBiEOG75TMBN.
PhylomeDBiQ8C1F4.
TreeFamiTF318303.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR008428. Chond_GalNAc.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF05679. CHGN. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 2 hits.

Sequencei

Sequence statusi: Complete.

Q8C1F4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRRGSILHS RTQWLLLGLA LLFSLVLFMY LLECAPQTDG NASLPGVVRE
60 70 80 90 100
NYGKEYYQAL LQEQEEHYQT RATSLKRQIA QLKQELQDMS EKMRALQERK
110 120 130 140 150
KLGANGVGYP GNREQAPSDL LEFLHSQIDR AEVSVGAKLP SEYGVVPFES
160 170 180 190 200
FTLMKVFQLE MGLTRHPEEK PVRKDKRDEL VEVIEAGVEV INNPDEDDAQ
210 220 230 240 250
EDEEGPLGEK LIFNENDFIE GYYRTERDKG TQYELFFKKA DLMEYRHVTL
260 270 280 290 300
FRPFGPLMKV KNELIDITRS VINIIVPLAE RTEAFSQFMQ NFRDVCIHQD
310 320 330 340 350
KRIHLTVVYF GKEGLSKVKS ILESVSSESD FHNYTLVSLD EEFNRGRGLN
360 370 380 390 400
VGARAWDKGE VLMFFCDVDI YFSAEFLNSC RLNAEPGKKV FYPVVFSLYN
410 420 430 440 450
PAIVYANQDV PPPVEQQLVH KKDSGFWRDF GFGMTCQYQS DFLSVGGFDM
460 470 480 490 500
EVKGWGGEDV HLYRKYLHGD LIVIRTPVPG LFHLWHEKHC ADELTPEQYR
510 520 530 540
MCIQSKAMNE ASHSHLGMMV FREEIEMHLR KQAYRTNSET AG
Length:542
Mass (Da):62,530
Last modified:March 1, 2003 - v1
Checksum:i974D37EB441419C7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti397 – 3971S → N in BAB31761 (PubMed:16141072).Curated
Sequence conflicti540 – 5401T → A in AAH23112 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK019496 mRNA. Translation: BAB31761.2.
AK028045 mRNA. Translation: BAC25717.1.
AC135861 Genomic DNA. No translation available.
BC023112 mRNA. Translation: AAH23112.2.
CCDSiCCDS20469.1.
RefSeqiNP_084441.3. NM_030165.3.
XP_006506839.1. XM_006506776.2.
XP_006506840.1. XM_006506777.2.
XP_006506841.1. XM_006506778.2.
UniGeneiMm.300317.

Genome annotation databases

EnsembliENSMUST00000049344; ENSMUSP00000039819; ENSMUSG00000042042.
GeneIDi78752.
KEGGimmu:78752.
UCSCiuc009dll.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK019496 mRNA. Translation: BAB31761.2.
AK028045 mRNA. Translation: BAC25717.1.
AC135861 Genomic DNA. No translation available.
BC023112 mRNA. Translation: AAH23112.2.
CCDSiCCDS20469.1.
RefSeqiNP_084441.3. NM_030165.3.
XP_006506839.1. XM_006506776.2.
XP_006506840.1. XM_006506777.2.
XP_006506841.1. XM_006506778.2.
UniGeneiMm.300317.

3D structure databases

ProteinModelPortaliQ8C1F4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000039819.

Protein family/group databases

CAZyiGT7. Glycosyltransferase Family 7.

Proteomic databases

EPDiQ8C1F4.
MaxQBiQ8C1F4.
PaxDbiQ8C1F4.
PRIDEiQ8C1F4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000049344; ENSMUSP00000039819; ENSMUSG00000042042.
GeneIDi78752.
KEGGimmu:78752.
UCSCiuc009dll.2. mouse.

Organism-specific databases

CTDi55454.
MGIiMGI:1926002. Csgalnact2.

Phylogenomic databases

eggNOGiKOG3588. Eukaryota.
ENOG410XNYM. LUCA.
GeneTreeiENSGT00760000119143.
HOGENOMiHOG000230628.
HOVERGENiHBG050930.
InParanoidiQ8C1F4.
KOiK00746.
OMAiNVGARAW.
OrthoDBiEOG75TMBN.
PhylomeDBiQ8C1F4.
TreeFamiTF318303.

Enzyme and pathway databases

ReactomeiR-MMU-2022870. Chondroitin sulfate biosynthesis.

Miscellaneous databases

NextBioi349435.
PROiQ8C1F4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C1F4.
ExpressionAtlasiQ8C1F4. baseline and differential.
GenevisibleiQ8C1F4. MM.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR008428. Chond_GalNAc.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF05679. CHGN. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver and Skin.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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] OF 380-542.
    Strain: Czech II.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiCGAT2_MOUSE
AccessioniPrimary (citable) accession number: Q8C1F4
Secondary accession number(s): Q6PAP6, Q8R5A2, Q9D2M1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: March 1, 2003
Last modified: March 16, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.