Reviewed, UniProtKB/Swiss-Prot P15907 (SIAT1_HUMAN)

Names and origin

Protein names

Recommended name:
    Beta-galactoside alpha-2,6-sialyltransferase 1
    EC=2.4.99.1
Alternative name(s):
    CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 1
      Short name=Alpha 2,6-ST
      Short name=Sialyltransferase 1
    ST6Gal I
    B-cell antigen CD75

Gene names

Name:	ST6GAL1
Synonyms:	SIAT1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	406 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Transfers sialic acid from the donor of substrate CMP-sialic acid to galactose containing acceptor substrates.
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.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Golgi apparatus › Golgi 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.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane Secreted
Domain	Signal-anchor Transmembrane
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	humoral immune response Traceable author statement. Source: ProtInc protein amino acid glycosylation Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to Golgi membrane Inferred from electronic annotation. Source: InterPro
Molecular function	beta-galactoside alpha-2,6-sialyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 406	406	Beta-galactoside alpha-2,6-sialyltransferase 1		PRO_0000149249
Regions
	Topological domain	1 – 9	9	Cytoplasmic
	Transmembrane	10 – 26	17	Signal-anchor for type II membrane protein Potential
	Topological domain	27 – 406	380	Lumenal Potential
Amino acid modifications
	Glycosylation	149	1	N-linked (GlcNAc...) Ref.8
	Glycosylation	161	1	N-linked (GlcNAc...) Ref.8
	Disulfide bond	184 ↔ 335		By similarity
Experimental info
	Sequence conflict	27	1	K → L in CAA38246. Ref.2
	Sequence conflict	72 – 73	2	HR → T in CAA38246. Ref.2
	Sequence conflict	144	1	L → P in CAA38246. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P15907-1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: AC1E24A3875CF00F	FASTA	406	46,605
	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

References

	« Hide 'large scale' referencesShow '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: 2408023] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[2]	"The B cell antigen CD75 is a cell surface sialytransferase." Stamenkovic I., Asheim H.C., Deggerdal A., Blomhoff H.K., Smeland E.B., Funderud S. J. Exp. Med. 172:641-643(1990) [PubMed: 2373995] [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: 1730763] [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. , 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: 14702039] [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. , 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: 15489334] [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: 2803295] [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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-149 AND ASN-161, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

ST6Gal I

Cross-references

Sequence databases
EMBLGenBankDDBJ	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. BC031476 mRNA. Translation: AAH31476.1. BC040009 mRNA. Translation: AAH40009.1.
IPI	IPI00013887.
PIR	A41734.
RefSeq	NP_003023.1. NP_775323.1. NP_775324.1.
UniGene	Hs.207459
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P15907.
Protein family/group databases
CAZy	GT29. Glycosyltransferase Family 29.
PTM databases
PhosphoSite	P15907.
Proteomic databases
PRIDE	P15907.
Genome annotation databases
Ensembl	ENST00000169298; ENSP00000169298; ENSG00000073849; Homo sapiens. [Genome view] ENST00000392479; ENSP00000376270; ENSG00000073849; Homo sapiens. [Genome view] ENST00000416235; ENSP00000414504; ENSG00000073849; Homo sapiens. [Genome view] ENST00000417392; ENSP00000407631; ENSG00000073849; Homo sapiens. [Genome view] ENST00000423451; ENSP00000411518; ENSG00000073849; Homo sapiens. [Genome view] ENST00000427315; ENSP00000412821; ENSG00000073849; Homo sapiens. [Genome view] ENST00000430309; ENSP00000399525; ENSG00000073849; Homo sapiens. [Genome view] ENST00000432152; ENSP00000407989; ENSG00000073849; Homo sapiens. [Genome view] ENST00000438590; ENSP00000416163; ENSG00000073849; Homo sapiens. [Genome view] ENST00000440338; ENSP00000388928; ENSG00000073849; Homo sapiens. [Genome view] ENST00000442023; ENSP00000403063; ENSG00000073849; Homo sapiens. [Genome view] ENST00000446170; ENSP00000388789; ENSG00000073849; Homo sapiens. [Genome view] ENST00000448044; ENSP00000389337; ENSG00000073849; Homo sapiens. [Genome view] ENST00000448408; ENSP00000390793; ENSG00000073849; Homo sapiens. [Genome view] ENST00000448449; ENSP00000415886; ENSG00000073849; Homo sapiens. [Genome view] ENST00000455441; ENSP00000397273; ENSG00000073849; Homo sapiens. [Genome view] ENST00000457772; ENSP00000412221; ENSG00000073849; Homo sapiens. [Genome view] ENST00000458216; ENSP00000400547; ENSG00000073849; Homo sapiens. [Genome view]
GeneID	6480.
KEGG	hsa:6480.
UCSC	uc003frb.1. human.
Organism-specific databases
CTD	6480.
GeneCards	GC03P188132.
H-InvDB	HIX0024271.
HGNC	HGNC:10860. ST6GAL1.
HPA	CAB016122.
MIM	109675. gene.
PharmGKB	PA35762.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P15907.
HOVERGEN	P15907.
OMA	APTANFQ.
Enzyme and pathway databases
BRENDA	2.4.99.1. 247.
Gene expression databases
ArrayExpress	P15907.
Bgee	P15907.
CleanEx	HS_ST6GAL1.
Genevestigator	P15907.
GermOnline	ENSG00000073849. 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 Resources
NextBio	25171.
SOURCE	Search...

Entry information

Entry name

SIAT1_HUMAN

Accession

Primary (citable) accession number: P15907
Secondary accession number(s): A8KA14

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	November 3, 2009
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.