Reviewed, UniProtKB/Swiss-Prot Q76K27 (SIAT2_MOUSE)

Names and origin

Protein names

Recommended name:
    Beta-galactoside alpha-2,6-sialyltransferase 2
      Short name=Alpha 2,6-ST 2
    EC=2.4.99.1
Alternative name(s):
    CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 2
    Sialyltransferase 2
    ST6Gal II
      Short name=ST6GalII

Gene names

Name:	St6gal2
Synonyms:	Kiaa1877

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	524 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Transfers sialic acid from the donor of substrate CMP-sialic acid to galactose containing acceptor substrates. Has alpha-2,6-sialyltransferase activity toward oligosaccharides that have the Gal-beta-1,4-GlcNAc sequence at the non-reducing end of their carbohydrate groups, but it has weak or no activities toward glycoproteins and glycolipids.
Catalytic activity	CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine = CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine. Ref.1
Subcellular location	Golgi apparatus › Golgi stack membrane; Single-pass type II membrane protein By similarity.
Tissue specificity	Mainly expressed in brain and embryo. Very low expression is also detected in spleen, oviduct, lung and skeletal muscle. Ref.1
Sequence similarities	Belongs to the glycosyltransferase 29 family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal-anchor Transmembrane
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Biological process	N-acetylneuraminate metabolic process Inferred by curator. Source: MGI oligosaccharide metabolic process Inferred from sequence or structural similarity. Source: UniProtKB protein amino acid glycosylation Inferred from electronic annotation. Source: InterPro
Cellular component	integral to Golgi membrane Inferred from electronic annotation. Source: InterPro
Molecular function	beta-galactoside alpha-2,6-sialyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q76K27-1)

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: Q76K27-2)

The sequence of this isoform differs from the canonical sequence as follows:
     436-438: ILI → TCV
     439-524: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 524	524	Beta-galactoside alpha-2,6-sialyltransferase 2		PRO_0000314786
Regions
	Topological domain	1 – 11	11	Cytoplasmic Potential
	Transmembrane	12 – 32	21	Signal-anchor for type II membrane protein Potential
	Topological domain	33 – 524	492	Lumenal Potential
	Compositional bias	230 – 262	33	Arg-rich
Amino acid modifications
	Glycosylation	302	1	N-linked (GlcNAc...) Potential
	Glycosylation	332	1	N-linked (GlcNAc...) Potential
	Glycosylation	520	1	N-linked (GlcNAc...) Potential
	Disulfide bond	291 ↔ 443		By similarity
Natural variations
	Alternative sequence	436 – 438	3	ILI → TCV in isoform 2.		VSP_030357
	Alternative sequence	439 – 524	86	Missing in isoform 2.		VSP_030358
Experimental info
	Sequence conflict	48	1	S → R in BAC38534. Ref.2
	Sequence conflict	48	1	S → R in AAI25587. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 68F1B225FAB3287D	FASTA	524	60,123
	10 20 30 40 50 60 MKPHLKQWRQ RMLFGIFVWG LLFLAIFIYF TNSNPAAPMP SSFSFLESRG LLPLQGKQRV 70 80 90 100 110 120 IMGALQEPSL PRSLDASKVL LDSHPENPFH PWPGDPQKWD QAPNGFDNGD EFFTSQVGRK 130 140 150 160 170 180 SQSAFYPEED SYFFVADQPE LYHHRQGALE LPSPGETSWR SGPVQPKQKL LHPRRGSLPE 190 200 210 220 230 240 EAYDSDMLSA SMSRAFLYRL WKGAVSSKML NPRLQKAMRY YMSFNKHGVR FRRRGRREAT 250 260 270 280 290 300 RTGPELLCEM RRRVRVRTLD GREAPFSGLG WRPLVPGVPL SQLHPRGLSS CAVVMSAGAI 310 320 330 340 350 360 LNSSLGEEID SHDAVLRFNS APTRGYEKDV GNKTTVRIIN SQILANPSHH FIDSALYKDV 370 380 390 400 410 420 ILVAWDPAPY SANLNLWYKK PDYNLFTPYI QHRRKYPTQP FYILHPKFIW QLWDIIQENT 430 440 450 460 470 480 REKIQPNPPS SGFIGILIMM SMCKEVHVYE YIPSVRQTEL CHYHELYYDA ACTLGAYHPL 490 500 510 520 LYEKLLVQRL NTGTQADLHH KGKVVLPGFQ TLRCPVTSPN NTHS
	Isoform 2. Checksum: 2B36EC61C71494A4	FASTA	438	50,213
	10 20 30 40 50 60 MKPHLKQWRQ RMLFGIFVWG LLFLAIFIYF TNSNPAAPMP SSFSFLESRG LLPLQGKQRV 70 80 90 100 110 120 IMGALQEPSL PRSLDASKVL LDSHPENPFH PWPGDPQKWD QAPNGFDNGD EFFTSQVGRK 130 140 150 160 170 180 SQSAFYPEED SYFFVADQPE LYHHRQGALE LPSPGETSWR SGPVQPKQKL LHPRRGSLPE 190 200 210 220 230 240 EAYDSDMLSA SMSRAFLYRL WKGAVSSKML NPRLQKAMRY YMSFNKHGVR FRRRGRREAT 250 260 270 280 290 300 RTGPELLCEM RRRVRVRTLD GREAPFSGLG WRPLVPGVPL SQLHPRGLSS CAVVMSAGAI 310 320 330 340 350 360 LNSSLGEEID SHDAVLRFNS APTRGYEKDV GNKTTVRIIN SQILANPSHH FIDSALYKDV 370 380 390 400 410 420 ILVAWDPAPY SANLNLWYKK PDYNLFTPYI QHRRKYPTQP FYILHPKFIW QLWDIIQENT 430 REKIQPNPPS SGFIGTCV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Comparison of the enzymatic properties of mouse beta-galactoside alpha2,6-sialyltransferases, ST6Gal I and II." Takashima S., Tsuji S., Tsujimoto M. J. Biochem. 134:287-296(2003) [PubMed: 12966079] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ENZYME ACTIVITY, TISSUE SPECIFICITY.
[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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6J. Tissue: Cerebellum.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[5]	"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H. DNA Res. 10:167-180(2003) [PubMed: 14621295] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 310-524 (ISOFORM 1). Tissue: Embryonic tail.
+	Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

ST6Gal II

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB095093 Genomic DNA. Translation: BAC87752.1. AK082566 mRNA. Translation: BAC38534.1. CT009635 Genomic DNA. Translation: CAP19182.1. BC125586 mRNA. Translation: AAI25587.1. AK129462 mRNA. Translation: BAC98272.1. Different initiation.
IPI	IPI00274908. IPI00881028.
RefSeq	NP_766417.1.
UniGene	Mm.311687
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GT29. Glycosyltransferase Family 29.
Proteomic databases
PRIDE	Q76K27.
Genome annotation databases
Ensembl	ENSMUST00000025000; ENSMUSP00000025000; ENSMUSG00000024172; Mus musculus. [Genome view] ENSMUST00000086878; ENSMUSP00000084091; ENSMUSG00000024172; Mus musculus. [Genome view]
GeneID	240119.
KEGG	mmu:240119.
Organism-specific databases
CTD	240119.
MGI	MGI:2445190. St6gal2.
Rouge	Search...
Phylogenomic databases
eggNOG	roNOG05993.
HOGENOM	HBG283896.
HOVERGEN	Q76K27.
InParanoid	Q76K27.
Enzyme and pathway databases
BRENDA	2.4.99.1. 244.
Gene expression databases
ArrayExpress	Q76K27.
Bgee	Q76K27.
CleanEx	MM_ST6GAL2.
Genevestigator	Q76K27.
Family and domain databases
InterPro	IPR011330. Glyco_hydro/deAcase_b/a-brl. IPR001675. Glyco_trans_29. [Graphical view]
Pfam	PF00777. Glyco_transf_29. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	384464.
SOURCE	Search...

Entry information

Entry name

SIAT2_MOUSE

Accession

Primary (citable) accession number: Q76K27
Secondary accession number(s): Q6ZPG5, Q8BUU4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	July 5, 2004
Last modified:	February 9, 2010
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)