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Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase (EC 2.4.99.8) (Alpha-2,8-sialyltransferase 8A) (Ganglioside GD3 synthase) (Ganglioside GT3 synthase) (Sialyltransferase 8A) (SIAT8-A) (Sialyltransferase St8Sia I) (ST8SiaI)

 SIA8A_HUMAN             Reviewed;         356 AA.
Q92185; A8K4H6; Q17RL0; Q6PZN5; Q93064;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
20-JUN-2018, entry version 155.
RecName: Full=Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase;
EC=2.4.99.8;
AltName: Full=Alpha-2,8-sialyltransferase 8A;
AltName: Full=Ganglioside GD3 synthase;
AltName: Full=Ganglioside GT3 synthase;
AltName: Full=Sialyltransferase 8A;
Short=SIAT8-A;
AltName: Full=Sialyltransferase St8Sia I;
Short=ST8SiaI;
Name=ST8SIA1; Synonyms=SIAT8, SIAT8A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND CATALYTIC
ACTIVITY.
TISSUE=Melanoma;
PubMed=8195250;
Sasaki K., Kurata K., Kojima N., Kurosawa N., Ohta S., Hanai N.,
Tsuji S., Nishi T.;
"Expression cloning of a GM3-specific alpha-2,8-sialyltransferase (GD3
synthase).";
J. Biol. Chem. 269:15950-15956(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND CATALYTIC
ACTIVITY.
TISSUE=Melanoma;
PubMed=8058740; DOI=10.1073/pnas.91.17.7952;
Nara K., Watanabe Y., Maruyama K., Kasahara K., Nagai Y., Sanai Y.;
"Expression cloning of a CMP-NeuAc:NeuAc alpha 2-3Gal beta 1-4Glc beta
1-1'Cer alpha 2,8-sialyltransferase (GD3 synthase) from human melanoma
cells.";
Proc. Natl. Acad. Sci. U.S.A. 91:7952-7956(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
AND TISSUE SPECIFICITY.
PubMed=7937974; DOI=10.1073/pnas.91.22.10455;
Haraguchi M., Yamashiro S., Yamamoto A., Furukawa K., Takamiya K.,
Lloyd K.O., Shiku H., Furukawa K.;
"Isolation of GD3 synthase gene by expression cloning of GM3 alpha-
2,8-sialyltransferase cDNA using anti-GD2 monoclonal antibody.";
Proc. Natl. Acad. Sci. U.S.A. 91:10455-10459(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
AND TISSUE SPECIFICITY.
PubMed=8631981;
Nakayama J., Fukuda M.N., Hirabayashi Y., Kanamori A., Sasaki K.,
Nishi T., Fukuda M.;
"Expression cloning of a human GT3 synthase. GD3 and GT3 are
synthesized by a single enzyme.";
J. Biol. Chem. 271:3684-3691(1996).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
Rimoldi S., Papis E., Bernardini G., Gornati R.;
"Cloning of alternative human SAT-2 mRNA.";
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
Konta L., Laws S.M., Riemenschneider M., Adamski J.;
"Alternative splice variant of the ST8SIA1 gene.";
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Stomach, and Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., 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., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
IDENTIFICATION.
PubMed=15843597; DOI=10.1093/glycob/cwi063;
Harduin-Lepers A., Mollicone R., Delannoy P., Oriol R.;
"The animal sialyltransferases and sialyltransferase-related genes: a
phylogenetic approach.";
Glycobiology 15:805-817(2005).
-!- FUNCTION: Involved in the production of gangliosides GD3 and GT3
from GM3; gangliosides are a subfamily of complex
glycosphinglolipds that contain one or more residues of sialic
acid. {ECO:0000269|PubMed:7937974, ECO:0000269|PubMed:8058740,
ECO:0000269|PubMed:8195250, ECO:0000269|PubMed:8631981}.
-!- CATALYTIC ACTIVITY: CMP-N-acetylneuraminate + alpha-N-
acetylneuraminyl-(2->3)-beta-D-galactosyl-R = CMP + alpha-N-
acetylneuraminyl-(2->8)-alpha-N-acetylneuraminyl-(2->3)-beta-D-
galactosyl-R. {ECO:0000269|PubMed:7937974,
ECO:0000269|PubMed:8058740, ECO:0000269|PubMed:8195250,
ECO:0000269|PubMed:8631981}.
-!- PATHWAY: Protein modification; protein glycosylation.
-!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305};
Single-pass type II membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q92185-1; Sequence=Displayed;
Name=2; Synonyms=Sat-2;
IsoId=Q92185-2; Sequence=VSP_047583, VSP_047584;
-!- TISSUE SPECIFICITY: Strongly expressed in melanoma cell lines,
adult and fetal brain and to a lesser extent in adult and fetal
lung. {ECO:0000269|PubMed:7937974, ECO:0000269|PubMed:8631981}.
-!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC37586.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAA54891.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=ST8Sia I;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_636";
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EMBL; X77922; CAA54891.1; ALT_INIT; mRNA.
EMBL; D26360; BAA05391.1; -; mRNA.
EMBL; L32867; AAA62366.1; -; mRNA.
EMBL; L43494; AAC37586.1; ALT_INIT; mRNA.
EMBL; AY569975; AAS75783.1; -; mRNA.
EMBL; EU041716; ABU62753.1; -; mRNA.
EMBL; AK290941; BAF83630.1; -; mRNA.
EMBL; AK315340; BAG37739.1; -; mRNA.
EMBL; AC007544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC007671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC053513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC087318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC138468; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471094; EAW96468.1; -; Genomic_DNA.
EMBL; BC117285; AAI17286.1; -; mRNA.
EMBL; BC126162; AAI26163.1; -; mRNA.
CCDS; CCDS8697.1; -. [Q92185-1]
PIR; A54032; A54032.
RefSeq; NP_001291379.1; NM_001304450.1.
RefSeq; NP_003025.1; NM_003034.3. [Q92185-1]
UniGene; Hs.408614; -.
ProteinModelPortal; Q92185; -.
SMR; Q92185; -.
BioGrid; 112380; 10.
STRING; 9606.ENSP00000379353; -.
SwissLipids; SLP:000000749; -.
SwissLipids; SLP:000000871; -.
CAZy; GT29; Glycosyltransferase Family 29.
iPTMnet; Q92185; -.
PhosphoSitePlus; Q92185; -.
SwissPalm; Q92185; -.
BioMuta; ST8SIA1; -.
PaxDb; Q92185; -.
PeptideAtlas; Q92185; -.
PRIDE; Q92185; -.
ProteomicsDB; 75252; -.
DNASU; 6489; -.
Ensembl; ENST00000261197; ENSP00000261197; ENSG00000111728. [Q92185-2]
Ensembl; ENST00000396037; ENSP00000379353; ENSG00000111728. [Q92185-1]
GeneID; 6489; -.
KEGG; hsa:6489; -.
UCSC; uc001rfo.4; human. [Q92185-1]
CTD; 6489; -.
DisGeNET; 6489; -.
EuPathDB; HostDB:ENSG00000111728.10; -.
GeneCards; ST8SIA1; -.
HGNC; HGNC:10869; ST8SIA1.
HPA; HPA026775; -.
MIM; 601123; gene.
neXtProt; NX_Q92185; -.
OpenTargets; ENSG00000111728; -.
PharmGKB; PA35770; -.
eggNOG; KOG2692; Eukaryota.
eggNOG; ENOG410XT8P; LUCA.
GeneTree; ENSGT00550000074407; -.
HOGENOM; HOG000090201; -.
HOVERGEN; HBG106106; -.
InParanoid; Q92185; -.
KO; K03371; -.
OMA; VYNHSYI; -.
OrthoDB; EOG091G0CER; -.
PhylomeDB; Q92185; -.
TreeFam; TF323961; -.
BioCyc; MetaCyc:HS03456-MONOMER; -.
BRENDA; 2.4.99.8; 2681.
Reactome; R-HSA-4085001; Sialic acid metabolism.
UniPathway; UPA00222; -.
UniPathway; UPA00378; -.
ChiTaRS; ST8SIA1; human.
GeneWiki; ST8SIA1; -.
GenomeRNAi; 6489; -.
PRO; PR:Q92185; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111728; -.
CleanEx; HS_ST8SIA1; -.
ExpressionAtlas; Q92185; baseline and differential.
Genevisible; Q92185; HS.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
GO; GO:0003828; F:alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity; TAS:Reactome.
GO; GO:0008373; F:sialyltransferase activity; TAS:ProtInc.
GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
GO; GO:0006688; P:glycosphingolipid biosynthetic process; TAS:ProtInc.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
Gene3D; 3.90.1480.20; -; 1.
InterPro; IPR001675; Glyco_trans_29.
InterPro; IPR038578; GT29-like_sf.
InterPro; IPR012163; Sialyl_trans.
Pfam; PF00777; Glyco_transf_29; 1.
PIRSF; PIRSF005557; Sialyl_trans; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Disulfide bond; Glycoprotein;
Glycosyltransferase; Golgi apparatus; Lipid metabolism; Membrane;
Reference proteome; Signal-anchor; Sphingolipid metabolism;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 356 Alpha-N-acetylneuraminide alpha-2,8-
sialyltransferase.
/FTId=PRO_0000149282.
TOPO_DOM 1 29 Cytoplasmic. {ECO:0000255}.
TRANSMEM 30 48 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 49 356 Lumenal. {ECO:0000255}.
REGION 188 190 Substrate binding.
{ECO:0000250|UniProtKB:O43173}.
REGION 274 276 Substrate binding.
{ECO:0000250|UniProtKB:O43173}.
ACT_SITE 322 322 Proton donor/acceptor.
{ECO:0000250|UniProtKB:O43173}.
BINDING 166 166 Substrate.
{ECO:0000250|UniProtKB:O43173}.
CARBOHYD 71 71 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 119 119 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 214 214 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 245 245 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 138 287 {ECO:0000250|UniProtKB:O43173}.
DISULFID 152 347 {ECO:0000250|UniProtKB:O43173}.
VAR_SEQ 128 135 ATPFQLPL -> MQSPSFVK (in isoform 2).
{ECO:0000303|Ref.5, ECO:0000303|Ref.6}.
/FTId=VSP_047583.
VAR_SEQ 136 356 Missing (in isoform 2).
{ECO:0000303|Ref.5, ECO:0000303|Ref.6}.
/FTId=VSP_047584.
SEQUENCE 356 AA; 40519 MW; 452FE04856964395 CRC64;
MSPCGRARRQ TSRGAMAVLA WKFPRTRLPM GASALCVVVL CWLYIFPVYR LPNEKEIVQG
VLQQGTAWRR NQTAARAFRK QMEDCCDPAH LFAMTKMNSP MGKSMWYDGE FLYSFTIDNS
TYSLFPQATP FQLPLKKCAV VGNGGILKKS GCGRQIDEAN FVMRCNLPPL SSEYTKDVGS
KSQLVTANPS IIRQRFQNLL WSRKTFVDNM KIYNHSYIYM PAFSMKTGTE PSLRVYYTLS
DVGANQTVLF ANPNFLRSIG KFWKSRGIHA KRLSTGLFLV SAALGLCEEV AIYGFWPFSV
NMHEQPISHH YYDNVLPFSG FHAMPEEFLQ LWYLHKIGAL RMQLDPCEDT SLQPTS


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EIAAB38440 Bos taurus,Bovine,CMP-NeuAc lactosylceramide alpha-2,3-sialyltransferase,Ganglioside GM3 synthase,Lactosylceramide alpha-2,3-sialyltransferase,Sialyltransferase 9,SIAT9,ST3Gal V,ST3GAL5,ST3GalV
EIAAB38441 CMP-NeuAc lactosylceramide alpha-2,3-sialyltransferase,Ganglioside GM3 synthase,Lactosylceramide alpha-2,3-sialyltransferase,Rat,Rattus norvegicus,Sialyltransferase 9,Siat9,ST3Gal V,St3gal5,ST3GalV
EIAAB38406 Alpha-2,8-sialyltransferase 8B,Rat,Rattus norvegicus,Sialyltransferase 8B,Sialyltransferase X,Sialytransferase St8Sia II,Siat8b,SIAT8-B,St8sia2,ST8SiaII,STX,Stx
EIAAB38405 Alpha-2,8-sialyltransferase 8B,Homo sapiens,Human,Sialyltransferase 8B,Sialyltransferase X,Sialytransferase St8Sia II,SIAT8B,SIAT8-B,ST8SIA2,ST8SiaII,STX,STX
EIAAB38398 Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 5,GalNAc alpha-2,6-sialyltransferase V,GD1 alpha synthase,Homo sapiens,Human,Sialyltransferase 7E,SIAT7E,SIAT7-E,ST6GalNAc V,ST6GALNAC5,ST6Gal
EIAAB38397 Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 5,GalNAc alpha-2,6-sialyltransferase V,GD1 alpha synthase,Mouse,Mus musculus,Sialyltransferase 7E,Siat7e,SIAT7-E,ST6GalNAc V,St6galnac5,ST6Gal
EIAAB38415 Alpha-2,8-sialyltransferase 8F,Mouse,Mus musculus,Sialyltransferase 8F,Sialytransferase St8Sia VI,Siat8f,SIAT8-F,St8sia6,ST8SiaVI
EIAAB38416 Alpha-2,8-sialyltransferase 8F,Homo sapiens,Human,Sialyltransferase 8F,Sialytransferase St8Sia VI,SIAT8F,SIAT8-F,ST8SIA6,ST8SiaVI
EIAAB38413 Alpha-2,8-sialyltransferase 8E,Homo sapiens,Human,Sialyltransferase 8E,Sialytransferase St8Sia V,SIAT8E,SIAT8-E,ST8SIA5,ST8SiaV
EIAAB38414 Alpha-2,8-sialyltransferase 8E,Mouse,Mus musculus,Sialyltransferase 8E,Sialytransferase St8Sia V,Siat8e,SIAT8-E,St8sia5,ST8SiaV,St8siav
EIAAB38390 Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2,Gal-beta-1,3-GalNAc alpha-2,6-sialyltransferase,GalNAc alpha-2,6-sialyltransferase II,Mouse,Mus musculus,Sialyltransferase 7B,Siat7,Siat7b,S
EIAAB38394 Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 3,GalNAc alpha-2,6-sialyltransferase III,Homo sapiens,Human,Sialyltransferase 7C,SIAT7C,SIAT7-C,ST6GalNAc III,ST6GALNAC3,ST6GalNAcIII,STY,UNQ2
EIAAB38387 Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1,GalNAc alpha-2,6-sialyltransferase I,Homo sapiens,Human,Sialyltransferase 7A,SIAT7A,SIAT7-A,ST6GalNAc I,ST6GALNAC1,ST6GalNAcI,UNQ543_PRO848
EIAAB38391 Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2,GalNAc alpha-2,6-sialyltransferase II,Homo sapiens,Human,Sialyltransferase 7B,SIAT7B,SIAT7-B,SIATL1,ST6GalNAc II,ST6GALNAC2,ST6GalNAcII,SThM


 

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