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Protein

CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2

Gene

St3gal2

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

Functioni

It may be responsible for the synthesis of the sequence NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc- found in terminal carbohydrate groups of certain glycoproteins, oligosaccharides and glycolipids. SIAT4A and SIAT4B sialylate the same acceptor substrates but exhibit different Km values.

Catalytic activityi

CMP-N-acetylneuraminate + beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R = CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R.

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei116 – 1161SubstrateBy similarity
Binding sitei157 – 1571SubstrateBy similarity
Binding sitei180 – 1801SubstrateBy similarity
Binding sitei240 – 2401SubstrateBy similarity
Binding sitei276 – 2761SubstrateBy similarity
Binding sitei280 – 2801Substrate; via amide nitrogenBy similarity
Binding sitei300 – 3001Substrate; via amide nitrogenBy similarity
Binding sitei309 – 3091SubstrateBy similarity
Binding sitei326 – 3261SubstrateBy similarity

GO - Molecular functioni

  • beta-galactoside (CMP) alpha-2,3-sialyltransferase activity Source: MGI

GO - Biological processi

  • protein glycosylation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiR-MMU-2022854. Keratan sulfate biosynthesis.
R-MMU-4085001. Sialic acid metabolism.
R-MMU-977068. Termination of O-glycan biosynthesis.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT29. Glycosyltransferase Family 29.

Chemistry

SwissLipidsiSLP:000001389.

Names & Taxonomyi

Protein namesi
Recommended name:
CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2 (EC:2.4.99.4)
Short name:
Alpha 2,3-ST 2
Short name:
Beta-galactoside alpha-2,3-sialyltransferase 2
Alternative name(s):
Gal-NAc6S
Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase
ST3Gal II
Short name:
ST3GalII
ST3GalA.2
Sialyltransferase 4B
Short name:
SIAT4-B
Gene namesi
Name:St3gal2
Synonyms:Siat4b, Siat5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:99427. St3gal2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence analysis
Transmembranei7 – 2721Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini28 – 350323LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 350350CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2PRO_0000149259Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi70 ↔ 75By similarity
Disulfide bondi72 ↔ 149By similarity
Glycosylationi92 – 921N-linked (GlcNAc...)Sequence analysis
Disulfide bondi152 ↔ 291By similarity
Glycosylationi211 – 2111N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

The soluble form derives from the membrane form by proteolytic processing.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ11204.
MaxQBiQ11204.
PaxDbiQ11204.
PRIDEiQ11204.

PTM databases

PhosphoSiteiQ11204.

Expressioni

Tissue specificityi

Strongly expressed in brain and liver and to a lesser extent in heart and kidney. Scarcely detectable in lung, pancreas, spleen and submaxillary gland.

Gene expression databases

BgeeiQ11204.
ExpressionAtlasiQ11204. baseline and differential.
GenevisibleiQ11204. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034197.

Structurei

3D structure databases

ProteinModelPortaliQ11204.
SMRiQ11204. Positions 68-349.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 29 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2692. Eukaryota.
ENOG410XT8P. LUCA.
GeneTreeiENSGT00760000119095.
HOGENOMiHOG000126811.
HOVERGENiHBG054227.
InParanoidiQ11204.
KOiK03368.
OMAiRCMGDAG.
TreeFamiTF354325.

Family and domain databases

InterProiIPR001675. Glyco_trans_29.
IPR012163. Sialyl_trans.
[Graphical view]
PfamiPF00777. Glyco_transf_29. 1 hit.
[Graphical view]
PIRSFiPIRSF005557. Sialyl_trans. 1 hit.

Sequencei

Sequence statusi: Complete.

Q11204-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKCSLRVWFL SMAFLLVFIM SLLFTYSHHS MATLPYLDSG ALGGTHRVKL
60 70 80 90 100
VPGYSGLQRL GKEGLLGRNC ACSRCMGDAS TSEWFDSHFD GNISPVWTRD
110 120 130 140 150
NMNLPPDVQR WWMMLQPQFK SHNTNEVLEK LFQIVPGENP YRFRDPQQCR
160 170 180 190 200
RCAVVGNSGN LRGSGYGQEV DSHNFIMRMN QAPTVGFEKD VGSRTTHHFM
210 220 230 240 250
YPESAKNLPA NVSFVLVPFK ALDLMWIASA LSTGQIRFTY APVKSFLRVD
260 270 280 290 300
KEKVQIYNPA FFKYIHDRWT EHHGRYPSTG MLVLFFALHV CDEVNVYGFG
310 320 330 340 350
ADSRGNWHHY WENNRYAGEF RKTGVHDADF EAHIIDMLAK ASKIEVYRGN
Length:350
Mass (Da):40,130
Last modified:July 27, 2011 - v2
Checksum:i3C59FA39E6A03E4D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti309 – 3102HY → RH in CAA54294 (PubMed:8144500).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76989 mRNA. Translation: CAA54294.1.
AK053827 mRNA. Translation: BAC35543.1.
AK131653 mRNA. Translation: BAE20742.1.
CH466525 Genomic DNA. Translation: EDL11478.1.
BC066064 mRNA. Translation: AAH66064.1.
CCDSiCCDS22667.1.
PIRiA54420.
RefSeqiNP_033205.2. NM_009179.3.
XP_006530849.1. XM_006530786.2.
XP_006530850.1. XM_006530787.1.
XP_006530851.1. XM_006530788.1.
UniGeneiMm.200388.

Genome annotation databases

EnsembliENSMUST00000034197; ENSMUSP00000034197; ENSMUSG00000031749.
GeneIDi20444.
KEGGimmu:20444.
UCSCiuc009nlk.2. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

ST3Gal II

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76989 mRNA. Translation: CAA54294.1.
AK053827 mRNA. Translation: BAC35543.1.
AK131653 mRNA. Translation: BAE20742.1.
CH466525 Genomic DNA. Translation: EDL11478.1.
BC066064 mRNA. Translation: AAH66064.1.
CCDSiCCDS22667.1.
PIRiA54420.
RefSeqiNP_033205.2. NM_009179.3.
XP_006530849.1. XM_006530786.2.
XP_006530850.1. XM_006530787.1.
XP_006530851.1. XM_006530788.1.
UniGeneiMm.200388.

3D structure databases

ProteinModelPortaliQ11204.
SMRiQ11204. Positions 68-349.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034197.

Chemistry

SwissLipidsiSLP:000001389.

Protein family/group databases

CAZyiGT29. Glycosyltransferase Family 29.

PTM databases

PhosphoSiteiQ11204.

Proteomic databases

EPDiQ11204.
MaxQBiQ11204.
PaxDbiQ11204.
PRIDEiQ11204.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034197; ENSMUSP00000034197; ENSMUSG00000031749.
GeneIDi20444.
KEGGimmu:20444.
UCSCiuc009nlk.2. mouse.

Organism-specific databases

CTDi6483.
MGIiMGI:99427. St3gal2.

Phylogenomic databases

eggNOGiKOG2692. Eukaryota.
ENOG410XT8P. LUCA.
GeneTreeiENSGT00760000119095.
HOGENOMiHOG000126811.
HOVERGENiHBG054227.
InParanoidiQ11204.
KOiK03368.
OMAiRCMGDAG.
TreeFamiTF354325.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiR-MMU-2022854. Keratan sulfate biosynthesis.
R-MMU-4085001. Sialic acid metabolism.
R-MMU-977068. Termination of O-glycan biosynthesis.

Miscellaneous databases

NextBioi298492.
PROiQ11204.
SOURCEiSearch...

Gene expression databases

BgeeiQ11204.
ExpressionAtlasiQ11204. baseline and differential.
GenevisibleiQ11204. MM.

Family and domain databases

InterProiIPR001675. Glyco_trans_29.
IPR012163. Sialyl_trans.
[Graphical view]
PfamiPF00777. Glyco_transf_29. 1 hit.
[Graphical view]
PIRSFiPIRSF005557. Sialyl_trans. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of cDNA for a new type of Gal beta 1,3GalNAc alpha 2,3-sialyltransferase."
    Lee Y.-C., Kojima N., Wada E., Kurosawa N., Nakaoka T., Hamamoto T., Tsuji S.
    J. Biol. Chem. 269:10028-10033(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "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: Cerebellum and Eye.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.

Entry informationi

Entry nameiSIA4B_MOUSE
AccessioniPrimary (citable) accession number: Q11204
Secondary accession number(s): Q8BPL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: May 11, 2016
This is version 120 of the entry and version 2 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.