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Q64685

- SIAT1_MOUSE

UniProt

Q64685 - SIAT1_MOUSE

Protein

Beta-galactoside alpha-2,6-sialyltransferase 1

Gene

St6gal1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    BRENDAi2.4.99.1. 3474.
    ReactomeiREACT_198565. N-Glycan antennae elongation.
    REACT_198575. Termination of O-glycan biosynthesis.
    REACT_202500. 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: 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.

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    2. Golgi cisterna membrane Source: UniProtKB-SubCell
    3. integral component of Golgi membrane Source: InterPro

    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

    PaxDbiQ64685.
    PRIDEiQ64685.

    PTM databases

    PhosphoSiteiQ64685.

    Miscellaneous databases

    PMAP-CutDBQ8K1L1.

    Expressioni

    Gene expression databases

    ArrayExpressiQ64685.
    BgeeiQ64685.
    CleanExiMM_ST6GAL1.
    GenevestigatoriQ64685.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000110992.

    Structurei

    3D structure databases

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

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 99CytoplasmicSequence Analysis
    Topological domaini27 – 403377LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei10 – 2617Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    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.
    InParanoidiQ8K1L1.
    KOiK00778.
    OMAiQVWNKDS.
    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

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    MIHTNLKRKF SCFVLVFLLF AIICVWKKGS DYEALTLQAK VFQMPKSQEK    50
    VAVGPAPQAV FSNSKQDPKE GVQILSYPRV TAKVKPQPSL QVWDKDSTYS 100
    KLNPRLLKIW RNYLNMNKYK VSYKGPGPGV KFSVEALRCH LRDHVNVSMI 150
    EATDFPFNTT EWEGYLPKEN FRTKAGPWHK CAVVSSAGSL KNSQLGREID 200
    NHDAVLRFNG APTDNFQQDV GTKTTIRLVN SQLVTTEKRF LKDSLYTEGI 250
    LILWDPSVYH ADIPQWYQKP DYNFFETYKS YRRLHPSQPF YILKPQMPWE 300
    LWDIIQEISP DLIQPNPPSS GMLGIIIMMT LCDQVDIYEF LPSKRKTDVC 350
    YYHQKFFDSA CTMGAYHPLL FEKNMVKHLN EGTDEDIYLF GKATLSGFRN 400
    NRC 403
    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:
    EMBL
    GenBank
    DDBJ
    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_006521873.1.
    XP_006521937.1. XM_006521874.1.
    XP_006521938.1. XM_006521875.1.
    XP_006521939.1. XM_006521876.1.
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS28077.1.
    RefSeqi NP_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.
    UniGenei Mm.149029.
    Mm.489708.

    3D structure databases

    ProteinModelPortali Q64685.
    SMRi Q64685. Positions 104-403.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000110992.

    Protein family/group databases

    CAZyi GT29. Glycosyltransferase Family 29.

    PTM databases

    PhosphoSitei Q64685.

    Proteomic databases

    PaxDbi Q64685.
    PRIDEi Q64685.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000023601 ; ENSMUSP00000023601 ; ENSMUSG00000022885 .
    ENSMUST00000115335 ; ENSMUSP00000110992 ; ENSMUSG00000022885 .
    ENSMUST00000178797 ; ENSMUSP00000136206 ; ENSMUSG00000022885 .
    GeneIDi 20440.
    KEGGi mmu:20440.
    UCSCi uc007yto.2. mouse.

    Organism-specific databases

    CTDi 6480.
    MGIi MGI:108470. St6gal1.

    Phylogenomic databases

    eggNOGi NOG249416.
    GeneTreei ENSGT00550000074444.
    HOGENOMi HOG000013206.
    HOVERGENi HBG052853.
    InParanoidi Q8K1L1.
    KOi K00778.
    OMAi QVWNKDS.
    OrthoDBi EOG741Z1S.
    TreeFami TF323961.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    BRENDAi 2.4.99.1. 3474.
    Reactomei REACT_198565. N-Glycan antennae elongation.
    REACT_198575. Termination of O-glycan biosynthesis.
    REACT_202500. Sialic acid metabolism.

    Miscellaneous databases

    NextBioi 298476.
    PMAP-CutDB Q8K1L1.
    PROi Q64685.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q64685.
    Bgeei Q64685.
    CleanExi MM_ST6GAL1.
    Genevestigatori Q64685.

    Family and domain databases

    InterProi IPR001675. Glyco_trans_29.
    IPR012163. Sialyl_trans.
    [Graphical view ]
    Pfami PF00777. Glyco_transf_29. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005557. Sialyl_trans. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    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: October 1, 2014
    This is version 116 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