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P15907 (SIAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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):
B-cell antigen CD75
CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 1
ST6Gal I
Short name=ST6GalI
Sialyltransferase 1
Gene names
Name:ST6GAL1
Synonyms:SIAT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transfers sialic acid from CMP-sialic acid to galactose-containing acceptor substrates. Ref.10 Ref.11

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. Ref.10 Ref.11

Enzyme regulation

Inhibited by CTP. Ref.11

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.

The HB-6, CDW75, and CD76 differentiation antigens are cell-surface carbohydrate determinants generated by this enzyme.

Sequence similarities

Belongs to the glycosyltransferase 29 family.

Biophysicochemical properties

Kinetic parameters:

KM=530 µM for CMP-NeuAc Ref.10

Vmax=1.074 pmol/min/µg enzyme

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 406406Beta-galactoside alpha-2,6-sialyltransferase 1
PRO_0000149249

Regions

Topological domain1 – 99Cytoplasmic
Transmembrane10 – 2617Helical; Signal-anchor for type II membrane protein; Potential
Topological domain27 – 406380Lumenal Potential
Region322 – 3243Substrate binding

Sites

Binding site1891Substrate; via amide nitrogen
Binding site2121Substrate
Binding site2331Substrate
Binding site3531Substrate; via carbonyl oxygen
Binding site3541Substrate
Binding site3651Substrate
Binding site3691Substrate Probable
Binding site3701Substrate
Binding site3761Substrate

Amino acid modifications

Modified residue3691Phosphotyrosine Ref.9
Glycosylation1491N-linked (GlcNAc...) Ref.8 Ref.11
Glycosylation1611N-linked (GlcNAc...) Ref.8
Disulfide bond142 ↔ 406 Ref.11
Disulfide bond184 ↔ 335 Ref.11
Disulfide bond353 ↔ 364 Ref.11

Experimental info

Sequence conflict271K → L in CAA38246. Ref.2
Sequence conflict72 – 732HR → T in CAA38246. Ref.2
Sequence conflict1441L → P in CAA38246. Ref.2

Secondary structure

.......................................................... 406
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15907 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: AC1E24A3875CF00F

FASTA40646,605
        10         20         30         40         50         60 
MIHTNLKKKF SCCVLVFLLF AVICVWKEKK KGSYYDSFKL QTKEFQVLKS LGKLAMGSDS 

        70         80         90        100        110        120 
QSVSSSSTQD PHRGRQTLGS LRGLAKAKPE ASFQVWNKDS SSKNLIPRLQ KIWKNYLSMN 

       130        140        150        160        170        180 
KYKVSYKGPG PGIKFSAEAL RCHLRDHVNV SMVEVTDFPF NTSEWEGYLP KESIRTKAGP 

       190        200        210        220        230        240 
WGRCAVVSSA GSLKSSQLGR EIDDHDAVLR FNGAPTANFQ QDVGTKTTIR LMNSQLVTTE 

       250        260        270        280        290        300 
KRFLKDSLYN EGILIVWDPS VYHSDIPKWY QNPDYNFFNN YKTYRKLHPN QPFYILKPQM 

       310        320        330        340        350        360 
PWELWDILQE ISPEEIQPNP PSSGMLGIII MMTLCDQVDI YEFLPSKRKT DVCYYYQKFF 

       370        380        390        400 
DSACTMGAYH PLLYEKNLVK HLNQGTDEDI YLLGKATLPG FRTIHC 

« Hide

References

« Hide 'large scale' references
[1]"Complete cDNA sequence encoding human beta-galactoside alpha-2,6-sialyltransferase."
Grundmann U.G., Nerlich C., Rein T., Zettlmeissl G.
Nucleic Acids Res. 18:667-667(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[2]"The B cell antigen CD75 is a cell surface sialyltransferase."
Stamenkovic I., Asheim H.C., Deggerdal A., Blomhoff H.K., Smeland E.B., Funderud S.
J. Exp. Med. 172:641-643(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The HB-6, CDw75, and CD76 differentiation antigens are unique cell-surface carbohydrate determinants generated by the beta-galactoside alpha 2,6-sialyltransferase."
Bast B.J.E.G., Zhou L.J., Freeman G.J., Colley K.J., Ernst T.J., Munro J.M., Tedder T.F.
J. Cell Biol. 116:423-435(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Spleen.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Trachea.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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].
Tissue: Lymph and Skin.
[7]"Isolation and characterization of a partial cDNA for a human sialyltransferase."
Lance P., Lau K.M., Lau J.T.Y.
Biochem. Biophys. Res. Commun. 164:225-232(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 74-406.
[8]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-149 AND ASN-161.
Tissue: Liver.
[9]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-369, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"Universal phosphatase-coupled glycosyltransferase assay."
Wu Z.L., Ethen C.M., Prather B., Machacek M., Jiang W.
Glycobiology 21:727-733(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[11]"The structure of human alpha-2,6-sialyltransferase reveals the binding mode of complex glycans."
Kuhn B., Benz J., Greif M., Engel A.M., Sobek H., Rudolph M.G.
Acta Crystallogr. D 69:1826-1838(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 89-406 IN COMPLEXES WITH CMP; CYTIDINE AND PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION AT ASN-149, DISULFIDE BONDS.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X17247 mRNA. Translation: CAA35111.1.
X54363 mRNA. Translation: CAA38246.1.
X62822 mRNA. Translation: CAA44634.1.
AK292879 mRNA. Translation: BAF85568.1.
CH471052 Genomic DNA. Translation: EAW78161.1.
CH471052 Genomic DNA. Translation: EAW78162.1.
CH471052 Genomic DNA. Translation: EAW78164.1.
BC031476 mRNA. Translation: AAH31476.1.
BC040009 mRNA. Translation: AAH40009.1.
PIRA41734.
RefSeqNP_003023.1. NM_003032.2.
NP_775323.1. NM_173216.2.
NP_775324.1. NM_173217.2.
XP_005247774.1. XM_005247717.1.
XP_005247776.1. XM_005247719.1.
XP_005247777.1. XM_005247720.1.
UniGeneHs.207459.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4JS1X-ray2.09A89-406[»]
4JS2X-ray2.30A89-406[»]
ProteinModelPortalP15907.
SMRP15907. Positions 89-406.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112374. 2 interactions.
IntActP15907. 1 interaction.
MINTMINT-5000509.
STRING9606.ENSP00000169298.

Protein family/group databases

CAZyGT29. Glycosyltransferase Family 29.

PTM databases

PhosphoSiteP15907.

Polymorphism databases

DMDM115445.

Proteomic databases

PaxDbP15907.
PRIDEP15907.

Protocols and materials databases

DNASU6480.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000169298; ENSP00000169298; ENSG00000073849.
ENST00000448044; ENSP00000389337; ENSG00000073849.
GeneID6480.
KEGGhsa:6480.
UCSCuc003frb.3. human.

Organism-specific databases

CTD6480.
GeneCardsGC03P186648.
HGNCHGNC:10860. ST6GAL1.
HPACAB015018.
CAB016122.
MIM109675. gene.
neXtProtNX_P15907.
PharmGKBPA35762.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG249416.
HOGENOMHOG000013206.
HOVERGENHBG052853.
InParanoidP15907.
KOK00778.
OMAQVWNKDS.
PhylomeDBP15907.
TreeFamTF323961.

Enzyme and pathway databases

BRENDA2.4.99.1. 2681.
ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressP15907.
BgeeP15907.
CleanExHS_ST6GAL1.
GenevestigatorP15907.

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

ChiTaRSST6GAL1. human.
GeneWikiST6GAL1.
GenomeRNAi6480.
NextBio25171.
PROP15907.
SOURCESearch...

Entry information

Entry nameSIAT1_HUMAN
AccessionPrimary (citable) accession number: P15907
Secondary accession number(s): A8KA14, D3DNV3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: April 16, 2014
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM