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Protein

Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2

Gene

St6galnac2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

CMP-N-acetylneuraminate + glycano-beta-D-galactosyl-1,3-(N-acetyl-D-galactosaminyl)-glycoprotein = CMP + glycano-beta-D-galactosyl-(2,6-alpha-N-acetylneuraminyl)-(N-acetyl-D-galactosaminyl)-glycoprotein.

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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

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

Protein family/group databases

CAZyiGT29. Glycosyltransferase Family 29.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2 (EC:2.4.99.-)
Alternative name(s):
Gal-beta-1,3-GalNAc alpha-2,6-sialyltransferase
GalNAc alpha-2,6-sialyltransferase II
ST6GalNAc II
Short name:
ST6GalNAcII
Sialyltransferase 7B
Short name:
SIAT7-B
Gene namesi
Name:St6galnac2
Synonyms:Siat7, Siat7b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:107553. St6galnac2.

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 – 373346LumenalSequence 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 – 373373Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2PRO_0000149273Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi103 – 1031N-linked (GlcNAc...)Sequence analysis
Disulfide bondi150 ↔ 316By similarity
Glycosylationi160 – 1601N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP70277.
PaxDbiP70277.
PRIDEiP70277.

PTM databases

PhosphoSiteiP70277.

Expressioni

Tissue specificityi

Highly expressed in lactating mammary gland and adult testis. Lower levels in kidney.

Gene expression databases

BgeeiP70277.
GenevisibleiP70277. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000078501.

Structurei

3D structure databases

ProteinModelPortaliP70277.
SMRiP70277. Positions 97-338.
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.
HOGENOMiHOG000231097.
HOVERGENiHBG056467.
InParanoidiP70277.
KOiK06616.
OMAiDKGDRPH.
OrthoDBiEOG7C8GH7.
PhylomeDBiP70277.
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.

P70277-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLPRRWLFR MLLLVATSSG ILLMLYSSAG QQSPETQVPA RNMAYPRAFF
60 70 80 90 100
DPKPPNSENR KSRLCQHSLS LAIQKDRRFR SLFDLSTPVL LWEGLFTQEL
110 120 130 140 150
WNNLSQHKVP YGWQGLSHEV IASTLRLLKS PESGELFGAP RKLPLSCIRC
160 170 180 190 200
AVVGNGGILN GSRQGQKIDA HDYVFRLNGA ITEGFERDVG TKTSFYGFTV
210 220 230 240 250
NTMKNSLISY AKLGFTSVPQ GQNLRYIFIP SSIRDYLMLR SAILGVPVPE
260 270 280 290 300
GPDKGDRPHT YFGPETSASK FKLLHPDFIS YLTERFLKSK LINTRFGDMY
310 320 330 340 350
MPSTGALMLL TALHTCDQVS AYGFITNNYQ KYSDHYFERE KKPLIFYANH
360 370
DLSLEASLWR DLHNAGILWL YQR
Length:373
Mass (Da):42,482
Last modified:August 16, 2004 - v2
Checksum:i4C1E6AE9AE618450
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti184 – 1841G → A in CAA63821 (PubMed:8662927).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X93999 mRNA. Translation: CAA63821.1.
X94000 Genomic DNA. Translation: CAA63822.1.
AK004613 mRNA. Translation: BAB23410.1.
AK136381 mRNA. Translation: BAE22955.1.
BC010208 mRNA. No translation available.
CCDSiCCDS36379.1.
RefSeqiNP_033206.2. NM_009180.3.
UniGeneiMm.3947.

Genome annotation databases

EnsembliENSMUST00000079545; ENSMUSP00000078501; ENSMUSG00000057286.
GeneIDi20446.
KEGGimmu:20446.
UCSCiuc007mma.1. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

ST6GalNAc II

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X93999 mRNA. Translation: CAA63821.1.
X94000 Genomic DNA. Translation: CAA63822.1.
AK004613 mRNA. Translation: BAB23410.1.
AK136381 mRNA. Translation: BAE22955.1.
BC010208 mRNA. No translation available.
CCDSiCCDS36379.1.
RefSeqiNP_033206.2. NM_009180.3.
UniGeneiMm.3947.

3D structure databases

ProteinModelPortaliP70277.
SMRiP70277. Positions 97-338.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000078501.

Protein family/group databases

CAZyiGT29. Glycosyltransferase Family 29.

PTM databases

PhosphoSiteiP70277.

Proteomic databases

MaxQBiP70277.
PaxDbiP70277.
PRIDEiP70277.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000079545; ENSMUSP00000078501; ENSMUSG00000057286.
GeneIDi20446.
KEGGimmu:20446.
UCSCiuc007mma.1. mouse.

Organism-specific databases

CTDi10610.
MGIiMGI:107553. St6galnac2.

Phylogenomic databases

eggNOGiKOG2692. Eukaryota.
ENOG410XT8P. LUCA.
GeneTreeiENSGT00760000119095.
HOGENOMiHOG000231097.
HOVERGENiHBG056467.
InParanoidiP70277.
KOiK06616.
OMAiDKGDRPH.
OrthoDBiEOG7C8GH7.
PhylomeDBiP70277.
TreeFamiTF354325.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiSt6galnac2. mouse.
NextBioi298502.
PROiP70277.
SOURCEiSearch...

Gene expression databases

BgeeiP70277.
GenevisibleiP70277. 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. "Molecular cloning and genomic analysis of mouse Galbeta1, 3GalNAc-specific GalNAc alpha2,6-sialyltransferase."
    Kurosawa N., Inoue M., Yoshida Y., Tsuji S.
    J. Biol. Chem. 271:15109-15116(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: ICR.
    Tissue: Submandibular gland.
  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: Lung.
  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].
    Strain: FVB/N.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiSIA7B_MOUSE
AccessioniPrimary (citable) accession number: P70277
Secondary accession number(s): Q3UWG0, Q9DC24
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: August 16, 2004
Last modified: May 11, 2016
This is version 121 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.