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Protein

Beta-galactoside alpha-2,6-sialyltransferase 1

Gene

ST6GAL1

Organism
Homo sapiens (Human)
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.2 Publications

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.2 Publications

Enzyme regulationi

Inhibited by CTP.1 Publication

Kineticsi

  1. KM=530 µM for CMP-NeuAc1 Publication
  1. Vmax=1.074 pmol/min/µg enzyme1 Publication

Pathway:iprotein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei189 – 1891Substrate; via amide nitrogen
Binding sitei212 – 2121Substrate
Binding sitei233 – 2331Substrate
Binding sitei353 – 3531Substrate; via carbonyl oxygen
Binding sitei354 – 3541Substrate
Binding sitei365 – 3651Substrate
Binding sitei369 – 3691SubstrateCurated
Binding sitei370 – 3701Substrate
Binding sitei376 – 3761Substrate

GO - Molecular functioni

  • beta-galactoside alpha-2,6-sialyltransferase activity Source: UniProtKB
  • sialyltransferase activity Source: UniProtKB

GO - Biological processi

  • cellular protein metabolic process Source: Reactome
  • dolichol-linked oligosaccharide biosynthetic process Source: Reactome
  • humoral immune response Source: ProtInc
  • N-acetylneuraminate metabolic process Source: UniProtKB
  • O-glycan processing Source: Reactome
  • post-translational protein modification Source: Reactome
  • protein N-linked glycosylation via asparagine Source: UniProtKB
  • protein O-linked glycosylation Source: Reactome
  • sialylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciMetaCyc:HS01118-MONOMER.
BRENDAi2.4.99.1. 2681.
ReactomeiREACT_115835. Termination of O-glycan biosynthesis.
REACT_25085. N-Glycan antennae elongation.
REACT_264366. 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):
B-cell antigen CD75
CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 1
ST6Gal I
Short name:
ST6GalI
Sialyltransferase 1
Gene namesi
Name:ST6GAL1
Synonyms:SIAT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:10860. ST6GAL1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99Cytoplasmic
Transmembranei10 – 2617Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini27 – 406380LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35762.

Polymorphism and mutation databases

BioMutaiST6GAL1.
DMDMi115445.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 406406Beta-galactoside alpha-2,6-sialyltransferase 1PRO_0000149249Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi142 ↔ 4061 Publication
Glycosylationi149 – 1491N-linked (GlcNAc...)2 Publications
Glycosylationi161 – 1611N-linked (GlcNAc...)1 Publication
Disulfide bondi184 ↔ 3351 Publication
Disulfide bondi353 ↔ 3641 Publication
Modified residuei369 – 3691Phosphotyrosine1 Publication

Post-translational modificationi

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.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP15907.
PaxDbiP15907.
PRIDEiP15907.

PTM databases

PhosphoSiteiP15907.

Expressioni

Gene expression databases

BgeeiP15907.
CleanExiHS_ST6GAL1.
ExpressionAtlasiP15907. baseline and differential.
GenevisibleiP15907. HS.

Organism-specific databases

HPAiCAB015018.
CAB016122.

Interactioni

Protein-protein interaction databases

BioGridi112374. 1 interaction.
IntActiP15907. 2 interactions.
MINTiMINT-5000509.
STRINGi9606.ENSP00000169298.

Structurei

Secondary structure

1
406
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi102 – 1043Combined sources
Helixi107 – 11812Combined sources
Helixi137 – 14711Combined sources
Turni158 – 1614Combined sources
Helixi163 – 1653Combined sources
Turni166 – 1683Combined sources
Helixi174 – 1774Combined sources
Beta strandi181 – 1877Combined sources
Helixi191 – 1933Combined sources
Helixi199 – 2024Combined sources
Beta strandi205 – 2117Combined sources
Helixi220 – 2234Combined sources
Beta strandi228 – 2336Combined sources
Helixi234 – 2396Combined sources
Helixi241 – 2444Combined sources
Helixi247 – 2504Combined sources
Beta strandi251 – 2577Combined sources
Helixi266 – 2716Combined sources
Helixi278 – 28710Combined sources
Beta strandi293 – 2964Combined sources
Helixi299 – 31113Combined sources
Beta strandi312 – 3143Combined sources
Helixi323 – 33412Combined sources
Beta strandi335 – 34410Combined sources
Beta strandi354 – 3563Combined sources
Helixi363 – 3664Combined sources
Beta strandi368 – 3703Combined sources
Helixi372 – 38211Combined sources
Helixi387 – 3937Combined sources
Beta strandi395 – 3995Combined sources
Helixi401 – 4033Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JS1X-ray2.09A89-406[»]
4JS2X-ray2.30A89-406[»]
ProteinModelPortaliP15907.
SMRiP15907. Positions 89-406.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni322 – 3243Substrate binding

Sequence similaritiesi

Belongs to the glycosyltransferase 29 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG249416.
GeneTreeiENSGT00550000074444.
HOGENOMiHOG000013206.
HOVERGENiHBG052853.
InParanoidiP15907.
KOiK00778.
OMAiSFQVWNK.
OrthoDBiEOG741Z1S.
PhylomeDBiP15907.
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.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P15907-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MIHTNLKKKF SCCVLVFLLF AVICVWKEKK KGSYYDSFKL QTKEFQVLKS
60 70 80 90 100
LGKLAMGSDS QSVSSSSTQD PHRGRQTLGS LRGLAKAKPE ASFQVWNKDS
110 120 130 140 150
SSKNLIPRLQ KIWKNYLSMN KYKVSYKGPG PGIKFSAEAL RCHLRDHVNV
160 170 180 190 200
SMVEVTDFPF NTSEWEGYLP KESIRTKAGP WGRCAVVSSA GSLKSSQLGR
210 220 230 240 250
EIDDHDAVLR FNGAPTANFQ QDVGTKTTIR LMNSQLVTTE KRFLKDSLYN
260 270 280 290 300
EGILIVWDPS VYHSDIPKWY QNPDYNFFNN YKTYRKLHPN QPFYILKPQM
310 320 330 340 350
PWELWDILQE ISPEEIQPNP PSSGMLGIII MMTLCDQVDI YEFLPSKRKT
360 370 380 390 400
DVCYYYQKFF DSACTMGAYH PLLYEKNLVK HLNQGTDEDI YLLGKATLPG

FRTIHC
Length:406
Mass (Da):46,605
Last modified:April 1, 1990 - v1
Checksum:iAC1E24A3875CF00F
GO
Isoform 2 (identifier: P15907-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-231: Missing.

Note: No experimental confirmation available.
Show »
Length:175
Mass (Da):20,764
Checksum:i2A31915E3D582F4B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271K → L in CAA38246 (PubMed:2373995).Curated
Sequence conflicti72 – 732HR → T in CAA38246 (PubMed:2373995).Curated
Sequence conflicti144 – 1441L → P in CAA38246 (PubMed:2373995).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 231231Missing in isoform 2. 1 PublicationVSP_056076Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17247 mRNA. Translation: CAA35111.1.
X54363 mRNA. Translation: CAA38246.1.
X62822 mRNA. Translation: CAA44634.1.
AK292879 mRNA. Translation: BAF85568.1.
AK312023 mRNA. Translation: BAG34960.1.
AC007488 Genomic DNA. No translation available.
AC007690 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78160.1.
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.
CCDSiCCDS3285.1. [P15907-1]
CCDS46973.1. [P15907-2]
PIRiA41734.
RefSeqiNP_003023.1. NM_003032.2. [P15907-1]
NP_775323.1. NM_173216.2. [P15907-1]
NP_775324.1. NM_173217.2. [P15907-2]
XP_005247774.1. XM_005247717.2. [P15907-1]
XP_005247776.1. XM_005247719.1. [P15907-1]
XP_005247777.1. XM_005247720.1. [P15907-1]
XP_006713797.1. XM_006713734.1. [P15907-1]
XP_011511387.1. XM_011513085.1. [P15907-1]
XP_011511388.1. XM_011513086.1. [P15907-1]
UniGeneiHs.207459.

Genome annotation databases

EnsembliENST00000169298; ENSP00000169298; ENSG00000073849.
ENST00000448044; ENSP00000389337; ENSG00000073849.
ENST00000457772; ENSP00000412221; ENSG00000073849. [P15907-2]
GeneIDi6480.
KEGGihsa:6480.
UCSCiuc003frb.3. human. [P15907-1]
uc003frc.3. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

ST6Gal I

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17247 mRNA. Translation: CAA35111.1.
X54363 mRNA. Translation: CAA38246.1.
X62822 mRNA. Translation: CAA44634.1.
AK292879 mRNA. Translation: BAF85568.1.
AK312023 mRNA. Translation: BAG34960.1.
AC007488 Genomic DNA. No translation available.
AC007690 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78160.1.
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.
CCDSiCCDS3285.1. [P15907-1]
CCDS46973.1. [P15907-2]
PIRiA41734.
RefSeqiNP_003023.1. NM_003032.2. [P15907-1]
NP_775323.1. NM_173216.2. [P15907-1]
NP_775324.1. NM_173217.2. [P15907-2]
XP_005247774.1. XM_005247717.2. [P15907-1]
XP_005247776.1. XM_005247719.1. [P15907-1]
XP_005247777.1. XM_005247720.1. [P15907-1]
XP_006713797.1. XM_006713734.1. [P15907-1]
XP_011511387.1. XM_011513085.1. [P15907-1]
XP_011511388.1. XM_011513086.1. [P15907-1]
UniGeneiHs.207459.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JS1X-ray2.09A89-406[»]
4JS2X-ray2.30A89-406[»]
ProteinModelPortaliP15907.
SMRiP15907. Positions 89-406.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112374. 1 interaction.
IntActiP15907. 2 interactions.
MINTiMINT-5000509.
STRINGi9606.ENSP00000169298.

Protein family/group databases

CAZyiGT29. Glycosyltransferase Family 29.

PTM databases

PhosphoSiteiP15907.

Polymorphism and mutation databases

BioMutaiST6GAL1.
DMDMi115445.

Proteomic databases

MaxQBiP15907.
PaxDbiP15907.
PRIDEiP15907.

Protocols and materials databases

DNASUi6480.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000169298; ENSP00000169298; ENSG00000073849.
ENST00000448044; ENSP00000389337; ENSG00000073849.
ENST00000457772; ENSP00000412221; ENSG00000073849. [P15907-2]
GeneIDi6480.
KEGGihsa:6480.
UCSCiuc003frb.3. human. [P15907-1]
uc003frc.3. human.

Organism-specific databases

CTDi6480.
GeneCardsiGC03P186648.
HGNCiHGNC:10860. ST6GAL1.
HPAiCAB015018.
CAB016122.
MIMi109675. gene.
neXtProtiNX_P15907.
PharmGKBiPA35762.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG249416.
GeneTreeiENSGT00550000074444.
HOGENOMiHOG000013206.
HOVERGENiHBG052853.
InParanoidiP15907.
KOiK00778.
OMAiSFQVWNK.
OrthoDBiEOG741Z1S.
PhylomeDBiP15907.
TreeFamiTF323961.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciMetaCyc:HS01118-MONOMER.
BRENDAi2.4.99.1. 2681.
ReactomeiREACT_115835. Termination of O-glycan biosynthesis.
REACT_25085. N-Glycan antennae elongation.
REACT_264366. Sialic acid metabolism.

Miscellaneous databases

ChiTaRSiST6GAL1. human.
GeneWikiiST6GAL1.
GenomeRNAii6480.
NextBioi25171.
PROiP15907.
SOURCEiSearch...

Gene expression databases

BgeeiP15907.
CleanExiHS_ST6GAL1.
ExpressionAtlasiP15907. baseline and differential.
GenevisibleiP15907. HS.

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. "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] (ISOFORM 1).
    Tissue: Placenta.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] (ISOFORM 1).
    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.
    , 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] (ISOFORMS 1 AND 2).
    Tissue: Thymus and Trachea.
  5. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORM 1).
    Tissue: Lymph and Skin.
  8. "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 (ISOFORM 1).
  9. "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.
  10. "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.
  11. "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.
  12. "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.

Entry informationi

Entry nameiSIAT1_HUMAN
AccessioniPrimary (citable) accession number: P15907
Secondary accession number(s): A8KA14, B2R513, D3DNV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 22, 2015
This is version 167 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.