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Q64685

- SIAT1_MOUSE

UniProt

Q64685 - SIAT1_MOUSE

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Protein
Beta-galactoside alpha-2,6-sialyltransferase 1
Gene
St6gal1, Siat1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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 nitrogen By similarity
Binding sitei209 – 2091Substrate By similarity
Binding sitei230 – 2301Substrate By similarity
Binding sitei350 – 3501Substrate; via carbonyl oxygen By similarity
Binding sitei351 – 3511Substrate By similarity
Binding sitei362 – 3621Substrate By similarity
Binding sitei366 – 3661Substrate By similarity
Binding sitei367 – 3671Substrate By similarity
Binding sitei373 – 3731Substrate By similarity

GO - Molecular functioni

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

GO - Biological processi

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

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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99Cytoplasmic Reviewed prediction
Transmembranei10 – 2617Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini27 – 403377Lumenal Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi cisterna membrane Source: UniProtKB-SubCell
  2. extracellular region 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 1
PRO_0000149250Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi139 ↔ 4031 Publication
Glycosylationi146 – 1461N-linked (GlcNAc...) Reviewed prediction
Glycosylationi158 – 1581N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi181 ↔ 3321 Publication
Disulfide bondi350 ↔ 3611 Publication
Modified residuei366 – 3661Phosphotyrosine By 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.

Family & Domainsi

Region

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

Sequence similaritiesi

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

« Hide

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti131 – 1311K → R in BAA03680. 1 Publication
Sequence conflicti136 – 1361A → G in BAA03680. 1 Publication
Sequence conflicti155 – 1551F → S in BAA03680. 1 Publication
Sequence conflicti170 – 1701N → T in BAA03680. 1 Publication
Sequence conflicti178 – 1792WH → CT in BAA03680. 1 Publication

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...

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

« 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(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: September 3, 2014
This is version 115 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

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