Q92185 (SIA8A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase
EC=2.4.99.8

Alternative name(s):
Alpha-2,8-sialyltransferase 8A
Ganglioside GD3 synthase
Ganglioside GT3 synthase
Sialyltransferase 8A
Short name=SIAT8-A
Sialyltransferase St8Sia I
Short name=ST8SiaI

Gene names

Name:	ST8SIA1
Synonyms:	SIAT8, SIAT8A

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	356 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.1 Ref.2 Ref.3 Ref.4
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. Ref.1 Ref.2 Ref.3 Ref.4
Pathway	Protein modification; protein glycosylation. Lipid metabolism; sphingolipid metabolism.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein Potential.
Tissue specificity	Strongly expressed in melanoma cell lines, adult and fetal brain and to a lesser extent in adult and fetal lung. Ref.3 Ref.4
Sequence similarities	Belongs to the glycosyltransferase 29 family.
Sequence caution	The sequence AAC37586.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA54891.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Lipid metabolism Sphingolipid metabolism
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Traceable author statement Ref.1. Source: ProtInc cellular response to heat Inferred from electronic annotation. Source: Compara glycosphingolipid biosynthetic process Traceable author statement Ref.1. Source: ProtInc positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara protein glycosylation Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	integral to Golgi membrane Inferred from electronic annotation. Source: InterPro integral to membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity Inferred from electronic annotation. Source: EC sialyltransferase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 356	356	Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase		PRO_0000149282
Regions
	Topological domain	1 – 29	29	Cytoplasmic Potential
	Transmembrane	30 – 48	19	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	49 – 356	308	Lumenal Potential
Amino acid modifications
	Glycosylation	71	1	N-linked (GlcNAc...) Potential
	Glycosylation	119	1	N-linked (GlcNAc...) Potential
	Glycosylation	214	1	N-linked (GlcNAc...) Potential
	Glycosylation	245	1	N-linked (GlcNAc...) Potential
	Disulfide bond	138 ↔ 287		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q92185 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 452FE04856964395	FASTA	356	40,519
	10 20 30 40 50 60 MSPCGRARRQ TSRGAMAVLA WKFPRTRLPM GASALCVVVL CWLYIFPVYR LPNEKEIVQG 70 80 90 100 110 120 VLQQGTAWRR NQTAARAFRK QMEDCCDPAH LFAMTKMNSP MGKSMWYDGE FLYSFTIDNS 130 140 150 160 170 180 TYSLFPQATP FQLPLKKCAV VGNGGILKKS GCGRQIDEAN FVMRCNLPPL SSEYTKDVGS 190 200 210 220 230 240 KSQLVTANPS IIRQRFQNLL WSRKTFVDNM KIYNHSYIYM PAFSMKTGTE PSLRVYYTLS 250 260 270 280 290 300 DVGANQTVLF ANPNFLRSIG KFWKSRGIHA KRLSTGLFLV SAALGLCEEV AIYGFWPFSV 310 320 330 340 350 NMHEQPISHH YYDNVLPFSG FHAMPEEFLQ LWYLHKIGAL RMQLDPCEDT SLQPTS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression cloning of a GM3-specific alpha-2,8-sialyltransferase (GD3 synthase)." Sasaki K., Kurata K., Kojima N., Kurosawa N., Ohta S., Hanai N., Tsuji S., Nishi T. J. Biol. Chem. 269:15950-15956(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY. Tissue: Melanoma.
[2]	"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." Nara K., Watanabe Y., Maruyama K., Kasahara K., Nagai Y., Sanai Y. Proc. Natl. Acad. Sci. U.S.A. 91:7952-7956(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY. Tissue: Melanoma.
[3]	"Isolation of GD3 synthase gene by expression cloning of GM3 alpha-2,8-sialyltransferase cDNA using anti-GD2 monoclonal antibody." Haraguchi M., Yamashiro S., Yamamoto A., Furukawa K., Takamiya K., Lloyd K.O., Shiku H., Furukawa K. Proc. Natl. Acad. Sci. U.S.A. 91:10455-10459(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
[4]	"Expression cloning of a human GT3 synthase. GD3 and GT3 are synthesized by a single enzyme." Nakayama J., Fukuda M.N., Hirabayashi Y., Kanamori A., Sasaki K., Nishi T., Fukuda M. J. Biol. Chem. 271:3684-3691(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
[5]	"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]. Tissue: Stomach and Teratocarcinoma.
[6]	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 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]. Tissue: Colon.
[8]	"The animal sialyltransferases and sialyltransferase-related genes: a phylogenetic approach." Harduin-Lepers A., Mollicone R., Delannoy P., Oriol R. Glycobiology 15:805-817(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION.
+	Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

ST8Sia I

Cross-references

Sequence databases
EMBL GenBank DDBJ	X77922 mRNA. Translation: CAA54891.1. Different initiation. D26360 mRNA. Translation: BAA05391.1. L32867 mRNA. Translation: AAA62366.1. L43494 mRNA. Translation: AAC37586.1. Different initiation. AK290941 mRNA. Translation: BAF83630.1. AK315340 mRNA. Translation: BAG37739.1. CH471094 Genomic DNA. Translation: EAW96468.1. BC117285 mRNA. Translation: AAI17286.1. BC126162 mRNA. Translation: AAI26163.1.
IPI	IPI00020197.
PIR	A54032.
RefSeq	NP_003025.1. NM_003034.3.
UniGene	Hs.408614.
3D structure databases
ProteinModelPortal	Q92185.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000379353.
Protein family/group databases
CAZy	GT29. Glycosyltransferase Family 29.
PTM databases
PhosphoSite	Q92185.
Polymorphism databases
DMDM	2494829.
Proteomic databases
PaxDb	Q92185.
PeptideAtlas	Q92185.
PRIDE	Q92185.
Protocols and materials databases
DNASU	6489.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000396037; ENSP00000379353; ENSG00000111728.
GeneID	6489.
KEGG	hsa:6489.
UCSC	uc001rfo.4. human.
Organism-specific databases
CTD	6489.
GeneCards	GC12M022119.
HGNC	HGNC:10869. ST8SIA1.
HPA	HPA026775.
MIM	601123. gene.
neXtProt	NX_Q92185.
PharmGKB	PA35770.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG272094.
HOGENOM	HOG000090201.
HOVERGEN	HBG106106.
InParanoid	Q92185.
KO	K03371.
OMA	HTSRGAM.
OrthoDB	EOG4NZTTK.
PhylomeDB	Q92185.
Enzyme and pathway databases
UniPathway	UPA00222. UPA00378.
Gene expression databases
ArrayExpress	Q92185.
Bgee	Q92185.
CleanEx	HS_ST8SIA1.
Genevestigator	Q92185.
GermOnline	ENSG00000111728. Homo sapiens.
Family and domain databases
InterPro	IPR001675. Glyco_trans_29. IPR012163. Sialyl_trans. [Graphical view]
Pfam	PF00777. Glyco_transf_29. 1 hit. [Graphical view]
PIRSF	PIRSF005557. Sialyl_trans. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	6489.
NextBio	25217.
SOURCE	Search...

Entry information

Entry name

SIA8A_HUMAN

Accession

Primary (citable) accession number: Q92185
Secondary accession number(s): A8K4H6, Q17RL0, Q93064

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.