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Protein

Beta-galactoside alpha-2,6-sialyltransferase 1

Gene

St6gal1

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

Functioni

Transfers sialic acid from CMP-sialic acid to galactose-containing acceptor substrates.

Catalytic activityi

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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei186 – 1861Substrate; via amide nitrogenBy similarity
Binding sitei209 – 2091SubstrateBy similarity
Binding sitei230 – 2301SubstrateBy similarity
Binding sitei350 – 3501Substrate; via carbonyl oxygenBy similarity
Binding sitei351 – 3511SubstrateBy similarity
Binding sitei362 – 3621SubstrateBy similarity
Binding sitei366 – 3661SubstrateBy similarity
Binding sitei367 – 3671SubstrateBy similarity
Binding sitei373 – 3731SubstrateBy similarity

GO - Molecular functioni

  1. beta-galactoside alpha-2,6-sialyltransferase activity Source: MGI
  2. sialyltransferase activity Source: MGI

GO - Biological processi

  1. N-acetylneuraminate metabolic process Source: UniProtKB
  2. protein glycosylation Source: MGI
  3. protein N-linked glycosylation via asparagine Source: UniProtKB
  4. sialylation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.4.99.1. 3474.
ReactomeiREACT_278748. Termination of O-glycan biosynthesis.
REACT_308816. N-Glycan antennae elongation.
REACT_310546. Sialic acid metabolism.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT29. Glycosyltransferase Family 29.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-galactoside alpha-2,6-sialyltransferase 1 (EC:2.4.99.1)
Short name:
Alpha 2,6-ST 1
Alternative name(s):
CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 1
ST6Gal I
Short name:
ST6GalI
Sialyltransferase 1
Gene namesi
Name:St6gal1
Synonyms:Siat1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:108470. St6gal1.

Subcellular locationi

Golgi apparatusGolgi stack membrane; Single-pass type II membrane protein. Secreted
Note: Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99CytoplasmicSequence Analysis
Transmembranei10 – 2617Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini27 – 403377LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular vesicular exosome Source: MGI
  2. Golgi cisterna membrane Source: UniProtKB-SubCell
  3. integral component of Golgi membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 403403Beta-galactoside alpha-2,6-sialyltransferase 1PRO_0000149250Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi139 ↔ 4031 Publication
Glycosylationi146 – 1461N-linked (GlcNAc...)Sequence Analysis
Glycosylationi158 – 1581N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi181 ↔ 3321 Publication
Disulfide bondi350 ↔ 3611 Publication
Modified residuei366 – 3661PhosphotyrosineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ64685.
PaxDbiQ64685.
PRIDEiQ64685.

PTM databases

PhosphoSiteiQ64685.

Miscellaneous databases

PMAP-CutDBQ8K1L1.

Expressioni

Gene expression databases

BgeeiQ64685.
CleanExiMM_ST6GAL1.
ExpressionAtlasiQ64685. baseline and differential.
GenevestigatoriQ64685.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000110992.

Structurei

3D structure databases

ProteinModelPortaliQ64685.
SMRiQ64685. Positions 104-403.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni319 – 3213Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyltransferase 29 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG249416.
GeneTreeiENSGT00550000074444.
HOGENOMiHOG000013206.
HOVERGENiHBG052853.
InParanoidiQ64685.
KOiK00778.
OMAiFQVWNKD.
OrthoDBiEOG741Z1S.
TreeFamiTF323961.

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.

Q64685-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIHTNLKRKF SCFVLVFLLF AIICVWKKGS DYEALTLQAK VFQMPKSQEK
60 70 80 90 100
VAVGPAPQAV FSNSKQDPKE GVQILSYPRV TAKVKPQPSL QVWDKDSTYS
110 120 130 140 150
KLNPRLLKIW RNYLNMNKYK VSYKGPGPGV KFSVEALRCH LRDHVNVSMI
160 170 180 190 200
EATDFPFNTT EWEGYLPKEN FRTKAGPWHK CAVVSSAGSL KNSQLGREID
210 220 230 240 250
NHDAVLRFNG APTDNFQQDV GTKTTIRLVN SQLVTTEKRF LKDSLYTEGI
260 270 280 290 300
LILWDPSVYH ADIPQWYQKP DYNFFETYKS YRRLHPSQPF YILKPQMPWE
310 320 330 340 350
LWDIIQEISP DLIQPNPPSS GMLGIIIMMT LCDQVDIYEF LPSKRKTDVC
360 370 380 390 400
YYHQKFFDSA CTMGAYHPLL FEKNMVKHLN EGTDEDIYLF GKATLSGFRN

NRC
Length:403
Mass (Da):46,586
Last modified:July 27, 2011 - v2
Checksum:iABBD86D8B13D3E04
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti131 – 1311K → R in BAA03680 (PubMed:8081843).Curated
Sequence conflicti136 – 1361A → G in BAA03680 (PubMed:8081843).Curated
Sequence conflicti155 – 1551F → S in BAA03680 (PubMed:8081843).Curated
Sequence conflicti170 – 1701N → T in BAA03680 (PubMed:8081843).Curated
Sequence conflicti178 – 1792WH → CT in BAA03680 (PubMed:8081843).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16106 mRNA. Translation: BAA03680.1.
AK084124 mRNA. Translation: BAC39120.1.
CH466521 Genomic DNA. Translation: EDK97666.1.
CH466521 Genomic DNA. Translation: EDK97667.1.
BC027833 mRNA. Translation: AAH27833.1.
BC092222 mRNA. Translation: AAH92222.1.
BC096026 mRNA. Translation: AAH96026.1.
CCDSiCCDS28077.1.
RefSeqiNP_001239434.1. NM_001252505.1.
NP_001239435.1. NM_001252506.1.
NP_666045.1. NM_145933.4.
XP_006521936.1. XM_006521873.2.
XP_006521937.1. XM_006521874.1.
XP_006521938.1. XM_006521875.2.
XP_006521939.1. XM_006521876.2.
UniGeneiMm.149029.
Mm.489708.

Genome annotation databases

EnsembliENSMUST00000023601; ENSMUSP00000023601; ENSMUSG00000022885.
ENSMUST00000115335; ENSMUSP00000110992; ENSMUSG00000022885.
ENSMUST00000178797; ENSMUSP00000136206; ENSMUSG00000022885.
GeneIDi20440.
KEGGimmu:20440.
UCSCiuc007yto.2. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

ST6Gal I

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16106 mRNA. Translation: BAA03680.1.
AK084124 mRNA. Translation: BAC39120.1.
CH466521 Genomic DNA. Translation: EDK97666.1.
CH466521 Genomic DNA. Translation: EDK97667.1.
BC027833 mRNA. Translation: AAH27833.1.
BC092222 mRNA. Translation: AAH92222.1.
BC096026 mRNA. Translation: AAH96026.1.
CCDSiCCDS28077.1.
RefSeqiNP_001239434.1. NM_001252505.1.
NP_001239435.1. NM_001252506.1.
NP_666045.1. NM_145933.4.
XP_006521936.1. XM_006521873.2.
XP_006521937.1. XM_006521874.1.
XP_006521938.1. XM_006521875.2.
XP_006521939.1. XM_006521876.2.
UniGeneiMm.149029.
Mm.489708.

3D structure databases

ProteinModelPortaliQ64685.
SMRiQ64685. Positions 104-403.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000110992.

Protein family/group databases

CAZyiGT29. Glycosyltransferase Family 29.

PTM databases

PhosphoSiteiQ64685.

Proteomic databases

MaxQBiQ64685.
PaxDbiQ64685.
PRIDEiQ64685.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023601; ENSMUSP00000023601; ENSMUSG00000022885.
ENSMUST00000115335; ENSMUSP00000110992; ENSMUSG00000022885.
ENSMUST00000178797; ENSMUSP00000136206; ENSMUSG00000022885.
GeneIDi20440.
KEGGimmu:20440.
UCSCiuc007yto.2. mouse.

Organism-specific databases

CTDi6480.
MGIiMGI:108470. St6gal1.

Phylogenomic databases

eggNOGiNOG249416.
GeneTreeiENSGT00550000074444.
HOGENOMiHOG000013206.
HOVERGENiHBG052853.
InParanoidiQ64685.
KOiK00778.
OMAiFQVWNKD.
OrthoDBiEOG741Z1S.
TreeFamiTF323961.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.99.1. 3474.
ReactomeiREACT_278748. Termination of O-glycan biosynthesis.
REACT_308816. N-Glycan antennae elongation.
REACT_310546. Sialic acid metabolism.

Miscellaneous databases

ChiTaRSiSt6gal1. mouse.
NextBioi298476.
PMAP-CutDBQ8K1L1.
PROiQ64685.
SOURCEiSearch...

Gene expression databases

BgeeiQ64685.
CleanExiMM_ST6GAL1.
ExpressionAtlasiQ64685. baseline and differential.
GenevestigatoriQ64685.

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. "Two step single primer mediated polymerase chain reaction. Application to cloning of putative mouse, beta-galactoside alpha 2,6-sialyltransferase cDNA."
    Hamamoto T., Kawasaki M., Kurosawa N., Nakaoka T., Lee Y.-C., Tsuji S.
    Bioorg. Med. Chem. 1:141-145(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain and Liver.
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Spinal ganglion.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUN-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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6 and FVB/N.
    Tissue: Mammary tumor.
  5. "Disulfide linkage in mouse ST6Gal I: Determination of linkage positions and mutant analysis."
    Hirano Y., Suzuki T., Matsumoto T., Ishihara Y., Takaki Y., Kono M., Dohmae N., Tsuji S.
    J. Biochem. 151:197-203(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.

Entry informationi

Entry nameiSIAT1_MOUSE
AccessioniPrimary (citable) accession number: Q64685
Secondary accession number(s): Q8K1L1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: April 1, 2015
This is version 122 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

External Data

Dasty 3

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 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.