SIA7F_HUMAN
ID SIA7F_HUMAN Reviewed; 333 AA.
AC Q969X2; B3KQ01; Q5T9C4; Q5T9C5; Q9H8A2; Q9ULB8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 6;
DE EC=2.4.99.- {ECO:0000269|PubMed:12668675, ECO:0000269|PubMed:17123352};
DE AltName: Full=GalNAc alpha-2,6-sialyltransferase VI;
DE AltName: Full=ST6GalNAc VI {ECO:0000303|PubMed:12668675, ECO:0000303|PubMed:17123352};
DE Short=ST6GalNAcVI;
DE Short=hST6GalNAc VI;
DE AltName: Full=Sialyltransferase 7F;
DE Short=SIAT7-F;
GN Name=ST6GALNAC6; Synonyms=SIAT7F; ORFNames=UNQ708/PRO1359;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=12668675; DOI=10.1074/jbc.m211034200;
RA Tsuchida A., Okajima T., Furukawa K., Ando T., Ishida H., Yoshida A.,
RA Nakamura Y., Kannagi R., Kiso M., Furukawa K.;
RT "Synthesis of disialyl Lewis a (Le(a)) structure in colon cancer cell lines
RT by a sialyltransferase, ST6GalNAc VI, responsible for the synthesis of
RT alpha-series gangliosides.";
RL J. Biol. Chem. 278:22787-22794(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=15843597; DOI=10.1093/glycob/cwi063;
RA Harduin-Lepers A., Mollicone R., Delannoy P., Oriol R.;
RT "The animal sialyltransferases and sialyltransferase-related genes: a
RT phylogenetic approach.";
RL Glycobiology 15:805-817(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Small intestine, and Thyroid;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP IDENTIFICATION.
RX PubMed=16207893; DOI=10.1093/glycob/cwj046;
RA Patel R.Y., Balaji P.V.;
RT "Identification of linkage-specific sequence motifs in
RT sialyltransferases.";
RL Glycobiology 16:108-116(2006).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=17123352; DOI=10.1042/bj20061118;
RA Senda M., Ito A., Tsuchida A., Hagiwara T., Kaneda T., Nakamura Y.,
RA Kasama K., Kiso M., Yoshikawa K., Katagiri Y., Ono Y., Ogiso M., Urano T.,
RA Furukawa K., Oshima S., Furukawa K.;
RT "Identification and expression of a sialyltransferase responsible for the
RT synthesis of disialylgalactosylgloboside in normal and malignant kidney
RT cells: downregulation of ST6GalNAc VI in renal cancers.";
RL Biochem. J. 402:459-470(2007).
RN [11]
RP REVIEW ON SIALYL LEWIS ANTIGENS.
RX PubMed=17760270;
RA Kannagi R.;
RT "Carbohydrate antigen sialyl Lewis a - its pathophysiological significance
RT and induction mechanism in cancer progression.";
RL Chang Gung Med. J. 30:189-209(2007).
CC -!- FUNCTION: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or
CC NeuAc) from CMP-NeuAc onto glycoproteins and glycolipids, forming an
CC alpha-2,6-linkage. Produces branched type disialyl structures by
CC transfer of a sialyl group onto the GalNAc or GlcNAc residue inside
CC backbone core chains having a terminal sialic acid with an alpha-2,3-
CC linkage on Gal. ST6GalNAcVI prefers glycolipids to glycoproteins,
CC predominantly catalyzing the biosynthesis of ganglioside GD1alpha from
CC GM1b (PubMed:12668675, PubMed:17123352). Besides GMb1, MSGG and other
CC glycolipids, it shows activity towards sialyl Lc4Cer generating
CC disialyl Lc4Cer, which can lead to the synthesis of disialyl Lewis a
CC (Le(a)), suggested to be a cancer-associated antigen (PubMed:12668675).
CC Also has activity toward GD1a and GT1b, and can generate DSGG
CC (disialylgalactosylgloboside) from MSGG (monosialylgalactosylgloboside)
CC (By similarity). {ECO:0000250|UniProtKB:Q9JM95,
CC ECO:0000269|PubMed:12668675, ECO:0000269|PubMed:17123352}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM1b (d18:1(4E)) =
CC a ganglioside GD1alpha (d18:1(4E)) + CMP + H(+);
CC Xref=Rhea:RHEA:41968, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:78568, ChEBI:CHEBI:78569;
CC Evidence={ECO:0000269|PubMed:12668675, ECO:0000269|PubMed:17123352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41969;
CC Evidence={ECO:0000305|PubMed:12668675, ECO:0000305|PubMed:17123352};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + N-acetyl-alpha-neuraminosyl-
CC (2->3)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-
CC beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-N-acyl-sphing-4-
CC enine = CMP + H(+) + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-
CC galactosyl-(1->3)-[N-acetyl-alpha-neuraminosyl-(2->6)]-N-acetyl-beta-
CC D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-
CC (1<->1')-N-acyl-sphing-4-enine; Xref=Rhea:RHEA:47884,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:88073, ChEBI:CHEBI:88079;
CC Evidence={ECO:0000269|PubMed:12668675, ECO:0000269|PubMed:17123352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47885;
CC Evidence={ECO:0000305|PubMed:12668675, ECO:0000305|PubMed:17123352};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + globoside MSGG = CMP +
CC globoside DSGG + H(+); Xref=Rhea:RHEA:56088, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:140623,
CC ChEBI:CHEBI:140624; Evidence={ECO:0000269|PubMed:17123352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56089;
CC Evidence={ECO:0000305|PubMed:17123352};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GD1a (d18:1(4E)) =
CC CMP + ganglioside GT1aalpha (d18:1(4E)) + H(+); Xref=Rhea:RHEA:41972,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:78445, ChEBI:CHEBI:78571;
CC Evidence={ECO:0000250|UniProtKB:Q9JM95};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41973;
CC Evidence={ECO:0000250|UniProtKB:Q9JM95};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GT1b (d18:1(4E)) =
CC CMP + ganglioside GQ1b alpha (d18:1(4E)) + H(+);
CC Xref=Rhea:RHEA:41976, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:78452, ChEBI:CHEBI:78572;
CC Evidence={ECO:0000250|UniProtKB:Q9JM95};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41977;
CC Evidence={ECO:0000250|UniProtKB:Q9JM95};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-[alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-alpha-D-GalNAc]-L-
CC Ser-[protein] + CMP-N-acetyl-beta-neuraminate = 3-O-{alpha-Neu5Ac-
CC (2->3)-beta-D-Gal-(1->3)-[alpha-Neu5Ac-(2->6)]-alpha-D-GalNAc}-L-Ser-
CC [protein] + CMP + H(+); Xref=Rhea:RHEA:65280, Rhea:RHEA-COMP:16760,
CC Rhea:RHEA-COMP:16761, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:156395, ChEBI:CHEBI:156397;
CC Evidence={ECO:0000269|PubMed:17123352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65281;
CC Evidence={ECO:0000305|PubMed:17123352};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-[alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-alpha-D-GalNAc]-L-
CC Thr-[protein] + CMP-N-acetyl-beta-neuraminate = 3-O-{alpha-Neu5Ac-
CC (2->3)-beta-D-Gal-(1->3)-[alpha-Neu5Ac-(2->6)]-alpha-D-GalNAc}-L-Thr-
CC [protein] + CMP + H(+); Xref=Rhea:RHEA:65284, Rhea:RHEA-COMP:16762,
CC Rhea:RHEA-COMP:16763, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:156396, ChEBI:CHEBI:156398;
CC Evidence={ECO:0000269|PubMed:17123352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65285;
CC Evidence={ECO:0000305|PubMed:17123352};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.33 mM for GM1b {ECO:0000269|PubMed:12668675};
CC KM=0.46 mM for sialyl Lc4Cer {ECO:0000269|PubMed:12668675};
CC -!- INTERACTION:
CC Q969X2; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-949146, EBI-12109402;
CC Q969X2; P54253: ATXN1; NbExp=7; IntAct=EBI-949146, EBI-930964;
CC Q969X2; Q7Z4F1: LRP10; NbExp=3; IntAct=EBI-949146, EBI-2830349;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q969X2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q969X2-2; Sequence=VSP_030359;
CC Name=3;
CC IsoId=Q969X2-3; Sequence=VSP_055722;
CC -!- TISSUE SPECIFICITY: Expressed in kidney, in proximal tubule epithelial
CC cells. Expressed in colon cell lines. {ECO:0000269|PubMed:12668675,
CC ECO:0000269|PubMed:17123352}.
CC -!- INDUCTION: Down-regulated in renal cancers.
CC -!- MISCELLANEOUS: The carbohydrate antigen disialyl Lewis a, which is at
CC least partly synthesized by ST6GALNAC6, is a normal counterpart of
CC sialyl Lewis a, better known as CA19-9, an antigen widely used as a
CC serum marker for diagnosis of cancers in the digestive track. Disialyl
CC Lewis a is predominantly expressed in non-malignant epithelial cells of
CC the digestive organs, while sialyl Lewis a is preferentially expressed
CC in cancers. Disialyl Lewis a in normal epithelial cells serves as a
CC ligand for immunosuppressive receptors, such as SIGLEC7 and SIGLEC9,
CC expressed on resident monocytes/macrophages and maintains immunological
CC homeostasis of mucosal membranes in digestive organs. Sialyl Lewis a,
CC as well as its positional isomer sialyl Lewis x, serves as a ligand for
CC vascular cell adhesion molecule E-selectin and facilitates hematogenous
CC metastasis through mediating adhesion of circulating cancer cells to
CC vascular endothelium (PubMed:17760270). {ECO:0000305|PubMed:17760270}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAW87712.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST6GalNAc
CC VI;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_635";
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DR EMBL; AJ507293; CAD45373.1; -; mRNA.
DR EMBL; AB035173; BAA87035.1; -; mRNA.
DR EMBL; AY358672; AAQ89035.1; -; mRNA.
DR EMBL; AK023900; BAB14715.1; -; mRNA.
DR EMBL; AK057100; BAG51863.1; -; mRNA.
DR EMBL; CR457318; CAG33599.1; -; mRNA.
DR EMBL; AL157935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87711.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87712.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471090; EAW87714.1; -; Genomic_DNA.
DR EMBL; BC006564; AAH06564.1; -; mRNA.
DR EMBL; BC007802; AAH07802.1; -; mRNA.
DR EMBL; BC016299; AAH16299.1; -; mRNA.
DR EMBL; BC036102; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS6882.1; -. [Q969X2-1]
DR CCDS; CCDS69668.1; -. [Q969X2-2]
DR CCDS; CCDS69669.1; -. [Q969X2-3]
DR RefSeq; NP_001273928.1; NM_001286999.1. [Q969X2-3]
DR RefSeq; NP_001273929.1; NM_001287000.1. [Q969X2-2]
DR RefSeq; NP_001273930.1; NM_001287001.1. [Q969X2-2]
DR RefSeq; NP_001273931.1; NM_001287002.1. [Q969X2-2]
DR RefSeq; NP_001273932.1; NM_001287003.1.
DR RefSeq; NP_038471.2; NM_013443.4. [Q969X2-1]
DR RefSeq; XP_011516912.1; XM_011518610.2. [Q969X2-1]
DR RefSeq; XP_011516913.1; XM_011518611.2. [Q969X2-2]
DR RefSeq; XP_016870148.1; XM_017014659.1. [Q969X2-3]
DR RefSeq; XP_016870154.1; XM_017014665.1. [Q969X2-2]
DR RefSeq; XP_016870155.1; XM_017014666.1. [Q969X2-2]
DR RefSeq; XP_016870156.1; XM_017014667.1. [Q969X2-2]
DR AlphaFoldDB; Q969X2; -.
DR BioGRID; 119039; 105.
DR IntAct; Q969X2; 5.
DR STRING; 9606.ENSP00000362235; -.
DR SwissLipids; SLP:000001366; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; Q969X2; 1 site.
DR iPTMnet; Q969X2; -.
DR PhosphoSitePlus; Q969X2; -.
DR BioMuta; ST6GALNAC6; -.
DR DMDM; 74751728; -.
DR jPOST; Q969X2; -.
DR MassIVE; Q969X2; -.
DR PaxDb; Q969X2; -.
DR PeptideAtlas; Q969X2; -.
DR PRIDE; Q969X2; -.
DR ProteomicsDB; 75868; -. [Q969X2-1]
DR ProteomicsDB; 75869; -. [Q969X2-2]
DR Antibodypedia; 17244; 94 antibodies from 21 providers.
DR DNASU; 30815; -.
DR Ensembl; ENST00000373141.5; ENSP00000362234.1; ENSG00000160408.16. [Q969X2-2]
DR Ensembl; ENST00000373142.5; ENSP00000362235.1; ENSG00000160408.16. [Q969X2-3]
DR Ensembl; ENST00000373144.7; ENSP00000362237.3; ENSG00000160408.16. [Q969X2-2]
DR Ensembl; ENST00000373146.6; ENSP00000362239.1; ENSG00000160408.16. [Q969X2-1]
DR Ensembl; ENST00000622357.5; ENSP00000477575.1; ENSG00000160408.16. [Q969X2-2]
DR GeneID; 30815; -.
DR KEGG; hsa:30815; -.
DR MANE-Select; ENST00000373146.6; ENSP00000362239.1; NM_013443.5; NP_038471.2.
DR UCSC; uc004bsn.3; human. [Q969X2-1]
DR CTD; 30815; -.
DR DisGeNET; 30815; -.
DR GeneCards; ST6GALNAC6; -.
DR HGNC; HGNC:23364; ST6GALNAC6.
DR HPA; ENSG00000160408; Low tissue specificity.
DR MIM; 610135; gene.
DR neXtProt; NX_Q969X2; -.
DR OpenTargets; ENSG00000160408; -.
DR OpenTargets; ENSG00000257524; -.
DR PharmGKB; PA134891331; -.
DR VEuPathDB; HostDB:ENSG00000160408; -.
DR GeneTree; ENSGT00940000160114; -.
DR HOGENOM; CLU_061099_3_0_1; -.
DR InParanoid; Q969X2; -.
DR OMA; XEQRSAV; -.
DR OrthoDB; 817470at2759; -.
DR PhylomeDB; Q969X2; -.
DR TreeFam; TF323961; -.
DR BRENDA; 2.4.99.7; 2681.
DR PathwayCommons; Q969X2; -.
DR Reactome; R-HSA-4085001; Sialic acid metabolism.
DR Reactome; R-HSA-9037629; Lewis blood group biosynthesis.
DR SignaLink; Q969X2; -.
DR BioGRID-ORCS; 30815; 13 hits in 1075 CRISPR screens.
DR GeneWiki; ST6GALNAC6; -.
DR GenomeRNAi; 30815; -.
DR Pharos; Q969X2; Tdark.
DR PRO; PR:Q969X2; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q969X2; protein.
DR Bgee; ENSG00000160408; Expressed in amygdala and 95 other tissues.
DR ExpressionAtlas; Q969X2; baseline and differential.
DR Genevisible; Q969X2; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; NAS:ProtInc.
DR GO; GO:0001665; F:alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase activity; ISS:BHF-UCL.
DR GO; GO:0008373; F:sialyltransferase activity; IDA:BHF-UCL.
DR GO; GO:0009988; P:cell-cell recognition; IC:BHF-UCL.
DR GO; GO:0001574; P:ganglioside biosynthetic process; ISS:BHF-UCL.
DR GO; GO:0009100; P:glycoprotein metabolic process; IDA:BHF-UCL.
DR GO; GO:0006687; P:glycosphingolipid metabolic process; IDA:BHF-UCL.
DR GO; GO:0006677; P:glycosylceramide metabolic process; IDA:BHF-UCL.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; ISS:BHF-UCL.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR Gene3D; 3.90.1480.20; -; 1.
DR InterPro; IPR001675; Glyco_trans_29.
DR InterPro; IPR038578; GT29-like_sf.
DR Pfam; PF00777; Glyco_transf_29; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Lipid metabolism; Membrane; Reference proteome;
KW Sialic acid; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..333
FT /note="Alpha-N-acetylgalactosaminide alpha-2,6-
FT sialyltransferase 6"
FT /id="PRO_0000314795"
FT TOPO_DOM 1..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..333
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 108..256
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..34
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12668675,
FT ECO:0000303|PubMed:12975309, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15843597, ECO:0000303|Ref.5"
FT /id="VSP_030359"
FT VAR_SEQ 272..333
FT /note="QRPRLQRMPYHYYEPKGPDECVTYIQNEHSRKGNHHRFITEKRVFSSWAQLY
FT GITFSHPSWT -> GPASSACPTTTTSPRGRTNVSPTSRMSTVARATTTASSPRKGSSH
FT RGPSCMASPSPTPPGPRPPSLWDLRRVRGEAASAQPLGQGPSSGQSRLAGVSPSQSGP
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055722"
FT CONFLICT 73
FT /note="L -> M (in Ref. 8; BC036102)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="R -> Q (in Ref. 8; BC036102)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="R -> Q (in Ref. 8; BC036102)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="M -> T (in Ref. 3; BAB14715)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 38068 MW; 5DB6FFA7D7A707C0 CRC64;
MACSRPPSQC EPTSLPPGPP AGRRHLPLSR RRREMSSNKE QRSAVFVILF ALITILILYS
SNSANEVFHY GSLRGRSRRP VNLKKWSITD GYVPILGNKT LPSRCHQCVI VSSSSHLLGT
KLGPEIERAE CTIRMNDAPT TGYSADVGNK TTYRVVAHSS VFRVLRRPQE FVNRTPETVF
IFWGPPSKMQ KPQGSLVRVI QRAGLVFPNM EAYAVSPGRM RQFDDLFRGE TGKDREKSHS
WLSTGWFTMV IAVELCDHVH VYGMVPPNYC SQRPRLQRMP YHYYEPKGPD ECVTYIQNEH
SRKGNHHRFI TEKRVFSSWA QLYGITFSHP SWT
