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Q64685 (SIAT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-galactoside alpha-2,6-sialyltransferase 1

Short name=Alpha 2,6-ST 1
EC=2.4.99.1
Alternative name(s):
CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 1
ST6Gal I
Short name=ST6GalI
Sialyltransferase 1
Gene names
Name:St6gal1
Synonyms:Siat1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length403 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

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.

Pathway

Protein modification; protein glycosylation.

Subcellular location

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.

Post-translational modification

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

Sequence similarities

Belongs to the glycosyltransferase 29 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 403403Beta-galactoside alpha-2,6-sialyltransferase 1
PRO_0000149250

Regions

Topological domain1 – 99Cytoplasmic Potential
Transmembrane10 – 2617Helical; Signal-anchor for type II membrane protein; Potential
Topological domain27 – 403377Lumenal Potential
Region319 – 3213Substrate binding By similarity

Sites

Binding site1861Substrate; via amide nitrogen By similarity
Binding site2091Substrate By similarity
Binding site2301Substrate By similarity
Binding site3501Substrate; via carbonyl oxygen By similarity
Binding site3511Substrate By similarity
Binding site3621Substrate By similarity
Binding site3661Substrate By similarity
Binding site3671Substrate By similarity
Binding site3731Substrate By similarity

Amino acid modifications

Modified residue3661Phosphotyrosine By similarity
Glycosylation1461N-linked (GlcNAc...) Potential
Glycosylation1581N-linked (GlcNAc...) Potential
Disulfide bond139 ↔ 403 Ref.5
Disulfide bond181 ↔ 332 Ref.5
Disulfide bond350 ↔ 361 Ref.5

Experimental info

Sequence conflict1311K → R in BAA03680. Ref.1
Sequence conflict1361A → G in BAA03680. Ref.1
Sequence conflict1551F → S in BAA03680. Ref.1
Sequence conflict1701N → T in BAA03680. Ref.1
Sequence conflict178 – 1792WH → CT in BAA03680. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q64685 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: ABBD86D8B13D3E04

FASTA40346,586
        10         20         30         40         50         60 
MIHTNLKRKF SCFVLVFLLF AIICVWKKGS DYEALTLQAK VFQMPKSQEK VAVGPAPQAV 

        70         80         90        100        110        120 
FSNSKQDPKE GVQILSYPRV TAKVKPQPSL QVWDKDSTYS KLNPRLLKIW RNYLNMNKYK 

       130        140        150        160        170        180 
VSYKGPGPGV KFSVEALRCH LRDHVNVSMI EATDFPFNTT EWEGYLPKEN FRTKAGPWHK 

       190        200        210        220        230        240 
CAVVSSAGSL KNSQLGREID NHDAVLRFNG APTDNFQQDV GTKTTIRLVN SQLVTTEKRF 

       250        260        270        280        290        300 
LKDSLYTEGI LILWDPSVYH ADIPQWYQKP DYNFFETYKS YRRLHPSQPF YILKPQMPWE 

       310        320        330        340        350        360 
LWDIIQEISP DLIQPNPPSS GMLGIIIMMT LCDQVDIYEF LPSKRKTDVC YYHQKFFDSA 

       370        380        390        400 
CTMGAYHPLL FEKNMVKHLN EGTDEDIYLF GKATLSGFRN NRC 

« Hide

References

« Hide 'large scale' references
[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(1993) [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. expand/collapse author list , 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: Spinal ganglion.
[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/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(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS28077.1.
RefSeqNP_001239434.1. NM_001252505.1.
NP_001239435.1. NM_001252506.1.
NP_666045.1. NM_145933.4.
XP_006521936.1. XM_006521873.1.
XP_006521937.1. XM_006521874.1.
XP_006521938.1. XM_006521875.1.
XP_006521939.1. XM_006521876.1.
UniGeneMm.149029.
Mm.489708.

3D structure databases

ProteinModelPortalQ64685.
SMRQ64685. Positions 104-403.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000110992.

Protein family/group databases

CAZyGT29. Glycosyltransferase Family 29.

PTM databases

PhosphoSiteQ64685.

Proteomic databases

PaxDbQ64685.
PRIDEQ64685.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023601; ENSMUSP00000023601; ENSMUSG00000022885.
ENSMUST00000115335; ENSMUSP00000110992; ENSMUSG00000022885.
ENSMUST00000178797; ENSMUSP00000136206; ENSMUSG00000022885.
GeneID20440.
KEGGmmu:20440.
UCSCuc007yto.2. mouse.

Organism-specific databases

CTD6480.
MGIMGI:108470. St6gal1.

Phylogenomic databases

eggNOGNOG249416.
GeneTreeENSGT00550000074444.
HOGENOMHOG000013206.
HOVERGENHBG052853.
InParanoidQ8K1L1.
KOK00778.
OMAQVWNKDS.
OrthoDBEOG741Z1S.
TreeFamTF323961.

Enzyme and pathway databases

BRENDA2.4.99.1. 3474.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ64685.
BgeeQ64685.
CleanExMM_ST6GAL1.
GenevestigatorQ64685.

Family and domain databases

InterProIPR001675. Glyco_trans_29.
IPR012163. Sialyl_trans.
[Graphical view]
PfamPF00777. Glyco_transf_29. 1 hit.
[Graphical view]
PIRSFPIRSF005557. Sialyl_trans. 1 hit.
ProtoNetSearch...

Other

NextBio298476.
PMAP-CutDBQ8K1L1.
PROQ64685.
SOURCESearch...

Entry information

Entry nameSIAT1_MOUSE
AccessionPrimary (citable) accession number: Q64685
Secondary accession number(s): Q8K1L1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot