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Q11203 (SIAT6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase

EC=2.4.99.6
Alternative name(s):
Beta-galactoside alpha-2,3-sialyltransferase 3
Short name=Alpha 2,3-ST 3
Gal beta-1,3(4) GlcNAc alpha-2,3 sialyltransferase
N-acetyllactosaminide alpha-2,3-sialyltransferase
ST3Gal III
Short name=ST3GalIII
ST3N
Sialyltransferase 6
Gene names
Name:ST3GAL3
Synonyms:SIAT6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the formation of the NeuAc-alpha-2,3-Gal-beta-1,4-GlcNAc-, NeuAc-alpha-2,3-Gal-beta-1,3-GlcNAc- or NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc- sequences found in terminal carbohydrate groups of glycoproteins and glycolipids. The highest activity is toward Gal-beta-1,3-GlcNAc and the lowest toward Gal-beta-1,3-GalNAc By similarity.

Catalytic activity

CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminyl-glycoprotein = CMP + alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminyl-glycoprotein.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatusGolgi stack membrane; Single-pass type II membrane protein. Secreted. Note: Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid.

Tissue specificity

Highly expressed in adult skeletal muscle and in all fetal tissues examined and to a much lesser extent in placenta, lung and liver.

Post-translational modification

The soluble form derives from the membrane form by proteolytic processing.

Involvement in disease

Mental retardation, autosomal recessive 12 (MRT12) [MIM:611090]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7

Epileptic encephalopathy, early infantile, 15 (EIEE15) [MIM:615006]: A form of epilepsy that manifests in the neonatal or the early infantile period as severely impaired cognitive and motor development, due to recurrent clinical seizures or prominent interictal epileptiform discharges. Patients develop infantile spasms, mainly of the flexor type, between 3 and 7 months of age, which are accompanied by hypsarrhythmia on EEG. Other features include poor eye contact, hypotonia, primitive reflexes, and irritability. Seizures evolve clinically to Lennox-Gastaut syndrome.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8

Sequence similarities

Belongs to the glycosyltransferase 29 family.

Ontologies

Keywords
   Cellular componentGolgi apparatus
Membrane
Secreted
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Epilepsy
Mental retardation
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processO-glycan processing

Traceable author statement. Source: Reactome

carbohydrate metabolic process

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

glycosaminoglycan metabolic process

Traceable author statement. Source: Reactome

keratan sulfate biosynthetic process

Traceable author statement. Source: Reactome

keratan sulfate metabolic process

Traceable author statement. Source: Reactome

post-translational protein modification

Traceable author statement. Source: Reactome

sialylation

Traceable author statement Ref.1. Source: GOC

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi cisterna membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Golgi membrane

Traceable author statement. Source: Reactome

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of Golgi membrane

Inferred from electronic annotation. Source: InterPro

   Molecular_functionN-acetyllactosaminide alpha-2,3-sialyltransferase activity

Traceable author statement Ref.1. Source: ProtInc

beta-galactoside (CMP) alpha-2,3-sialyltransferase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 26 isoforms produced by alternative splicing. [Align] [Select]
Isoform B1 (identifier: Q11203-1)

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.
Isoform A1 (identifier: Q11203-2)

The sequence of this isoform differs from the canonical sequence as follows:
     40-40: N → SKYSHSSSPQEKPVAD
Isoform A7 (identifier: Q11203-3)

The sequence of this isoform differs from the canonical sequence as follows:
     40-40: N → SKYSHSSSPQEKPVAD
     133-155: DNLIKAILSVTKEYRLTPALDSL → VLDAQYPARERVSAEAGESSRHH
     156-375: Missing.
Isoform A8 (identifier: Q11203-4)

The sequence of this isoform differs from the canonical sequence as follows:
     40-40: N → SKYSHSSSPQEKPVAD
     70-70: L → LSPRTLCTVVFGLDCILESPGEPKKLLMPASHPLEILKSLSEDTAFALGFLKLPR
Isoform B1-90 (identifier: Q11203-5)

The sequence of this isoform differs from the canonical sequence as follows:
     249-278: Missing.
Isoform B1+32 (identifier: Q11203-6)

The sequence of this isoform differs from the canonical sequence as follows:
     187-189: LNS → PRL
     190-375: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform B3 (identifier: Q11203-7)

The sequence of this isoform differs from the canonical sequence as follows:
     71-101: Missing.
Isoform B4 (identifier: Q11203-8)

The sequence of this isoform differs from the canonical sequence as follows:
     249-346: Missing.
Isoform B4+173 (identifier: Q11203-9)

The sequence of this isoform differs from the canonical sequence as follows:
     102-115: FSKPAPMFLDDSFR → EKVRTFMAWLAWYG
     116-375: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform B5+26 (identifier: Q11203-10)

The sequence of this isoform differs from the canonical sequence as follows:
     187-375: Missing.
Isoform B5+173 (identifier: Q11203-11)

The sequence of this isoform differs from the canonical sequence as follows:
     102-121: FSKPAPMFLDDSFRKWARIR → AKRNGAWRQKHIQAYVLRQR
     122-375: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform B7 (identifier: Q11203-12)

The sequence of this isoform differs from the canonical sequence as follows:
     133-155: DNLIKAILSVTKEYRLTPALDSL → VLDAQYPARERVSAEAGESSRHH
     156-375: Missing.
Isoform B8 (identifier: Q11203-13)

The sequence of this isoform differs from the canonical sequence as follows:
     70-70: L → LSPRTLCTVVFGLDCILESPGEPKKLLMPASHPLEILKSLSEDTAFALGFLKLPR
Isoform B10 (identifier: Q11203-14)

The sequence of this isoform differs from the canonical sequence as follows:
     133-151: DNLIKAILSVTKEYRLTPA → ECIGWLLEICGHSSAQGAP
     152-375: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform C1 (identifier: Q11203-15)

The sequence of this isoform differs from the canonical sequence as follows:
     40-56: NSVVLSFDSAGQTLGSE → K
Isoform C4 (identifier: Q11203-16)

The sequence of this isoform differs from the canonical sequence as follows:
     40-56: NSVVLSFDSAGQTLGSE → K
     249-346: Missing.
Isoform C5 (identifier: Q11203-17)

The sequence of this isoform differs from the canonical sequence as follows:
     40-56: NSVVLSFDSAGQTLGSE → K
     186-202: RLNSAPVKGFEKDVGSK → SPGRTISSERKSFCGSW
     203-375: Missing.
Isoform C7 (identifier: Q11203-18)

The sequence of this isoform differs from the canonical sequence as follows:
     40-56: NSVVLSFDSAGQTLGSE → K
     133-155: DNLIKAILSVTKEYRLTPALDSL → VLDAQYPARERVSAEAGESSRHH
     156-375: Missing.
Isoform C8 (identifier: Q11203-19)

The sequence of this isoform differs from the canonical sequence as follows:
     40-56: NSVVLSFDSAGQTLGSE → K
     70-70: L → LSPRTLCTVVFGLDCILESPGEPKKLLMPASHPLEILKSLSEDTAFALGFLKLPR
Isoform C9 (identifier: Q11203-20)

The sequence of this isoform differs from the canonical sequence as follows:
     40-56: NSVVLSFDSAGQTLGSE → K
     187-244: LNSAPVKGFE...DFKWLKYIVY → VHRMASGNLW...GTSLPLAVWQ
     245-375: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform C11 (identifier: Q11203-21)

The sequence of this isoform differs from the canonical sequence as follows:
     40-56: NSVVLSFDSAGQTLGSE → K
     71-101: Missing.
     249-346: Missing.
Isoform C12 (identifier: Q11203-22)

The sequence of this isoform differs from the canonical sequence as follows:
     40-56: NSVVLSFDSAGQTLGSE → K
     102-117: FSKPAPMFLDDSFRKW → PGRTISSERKSFCGSW
     118-375: Missing.
Isoform D2+26 (identifier: Q11203-23)

The sequence of this isoform differs from the canonical sequence as follows:
     40-55: NSVVLSFDSAGQTLGS → SKYSHSSSPQEKPVA
     187-375: Missing.
Isoform D5 (identifier: Q11203-24)

The sequence of this isoform differs from the canonical sequence as follows:
     40-55: NSVVLSFDSAGQTLGS → SKYSHSSSPQEKPVA
     186-202: RLNSAPVKGFEKDVGSK → SPGRTISSERKSFCGSW
     203-375: Missing.
Isoform E1 (identifier: Q11203-25)

The sequence of this isoform differs from the canonical sequence as follows:
     40-43: NSVV → SLLN
     44-375: Missing.
Isoform E3+32 (identifier: Q11203-26)

The sequence of this isoform differs from the canonical sequence as follows:
     40-73: NSVVLSFDSAGQTLGSEYDRLGFLLNLDSKLPAE → SSPSQHPCSWMTPFASGLESGSSCRLLGSKVKTI
     74-375: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 375375CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase
PRO_0000149266

Regions

Topological domain1 – 88Cytoplasmic Potential
Transmembrane9 – 2820Helical; Signal-anchor for type II membrane protein; Potential
Topological domain29 – 375347Lumenal Potential

Amino acid modifications

Glycosylation801N-linked (GlcNAc...) Potential
Glycosylation1711N-linked (GlcNAc...) Potential
Disulfide bond160 ↔ 314 By similarity

Natural variations

Alternative sequence40 – 7334NSVVL…KLPAE → SSPSQHPCSWMTPFASGLES GSSCRLLGSKVKTI in isoform E3+32.
VSP_010595
Alternative sequence40 – 5617NSVVL…TLGSE → K in isoform C1, isoform C4, isoform C5, isoform C7, isoform C8, isoform C9, isoform C11 and isoform C12.
VSP_010594
Alternative sequence40 – 5516NSVVL…QTLGS → SKYSHSSSPQEKPVA in isoform D5 and isoform D2+26.
VSP_010593
Alternative sequence40 – 434NSVV → SLLN in isoform E1.
VSP_010592
Alternative sequence401N → SKYSHSSSPQEKPVAD in isoform A1, isoform A7 and isoform A8.
VSP_010591
Alternative sequence44 – 375332Missing in isoform E1.
VSP_010596
Alternative sequence701L → LSPRTLCTVVFGLDCILESP GEPKKLLMPASHPLEILKSL SEDTAFALGFLKLPR in isoform A8, isoform B8 and isoform C8.
VSP_010597
Alternative sequence71 – 10131Missing in isoform B3 and isoform C11.
VSP_010598
Alternative sequence74 – 375302Missing in isoform E3+32.
VSP_010599
Alternative sequence102 – 12120FSKPA…WARIR → AKRNGAWRQKHIQAYVLRQR in isoform B5+173.
VSP_010602
Alternative sequence102 – 11716FSKPA…SFRKW → PGRTISSERKSFCGSW in isoform C12.
VSP_010601
Alternative sequence102 – 11514FSKPA…DDSFR → EKVRTFMAWLAWYG in isoform B4+173.
VSP_010600
Alternative sequence116 – 375260Missing in isoform B4+173.
VSP_010603
Alternative sequence118 – 375258Missing in isoform C12.
VSP_010604
Alternative sequence122 – 375254Missing in isoform B5+173.
VSP_010605
Alternative sequence133 – 15523DNLIK…ALDSL → VLDAQYPARERVSAEAGESS RHH in isoform A7, isoform B7 and isoform C7.
VSP_010607
Alternative sequence133 – 15119DNLIK…RLTPA → ECIGWLLEICGHSSAQGAP in isoform B10.
VSP_010606
Alternative sequence152 – 375224Missing in isoform B10.
VSP_010608
Alternative sequence156 – 375220Missing in isoform A7, isoform B7 and isoform C7.
VSP_010609
Alternative sequence186 – 20217RLNSA…DVGSK → SPGRTISSERKSFCGSW in isoform C5 and isoform D5.
VSP_010610
Alternative sequence187 – 375189Missing in isoform B5+26 and isoform D2+26.
VSP_010613
Alternative sequence187 – 24458LNSAP…KYIVY → VHRMASGNLWPLECPRSPLR FESSTHISSRRPPSPSLACP STMASWAGGTSLPLAVWQ in isoform C9.
VSP_010612
Alternative sequence187 – 1893LNS → PRL in isoform B1+32.
VSP_010611
Alternative sequence190 – 375186Missing in isoform B1+32.
VSP_010614
Alternative sequence203 – 375173Missing in isoform C5 and isoform D5.
VSP_010615
Alternative sequence245 – 375131Missing in isoform C9.
VSP_010616
Alternative sequence249 – 34698Missing in isoform B4, isoform C4 and isoform C11.
VSP_010618
Alternative sequence249 – 27830Missing in isoform B1-90.
VSP_010617
Natural variant131A → D in MRT12; most of the mutant protein is improperly localized to the endoplasmic reticulum preventing the protein from interacting with its substrates in the Golgi and resulting in a loss-of-function. Ref.7
VAR_066594
Natural variant3201A → P in EIEE15. Ref.8
VAR_069319
Natural variant3701D → Y in MRT12; the mutant protein is improperly localized to the endoplasmic reticulum preventing the protein from interacting with its substrates in the Golgi and resulting in a loss-of-function; shows a complete lack of enzyme activity; secretion of the mutant protein is dramatically reduced compared to wild-type. Ref.7
VAR_066595

Experimental info

Sequence conflict381D → N in AAO38806. Ref.3
Sequence conflict941L → S in AAO38810. Ref.3
Sequence conflict1231F → L in AAO38810. Ref.3
Sequence conflict3511N → S in AAO38811. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform B1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: C9B7B61AD580EC2E

FASTA37542,171
        10         20         30         40         50         60 
MGLLVFVRNL LLALCLFLVL GFLYYSAWKL HLLQWEEDSN SVVLSFDSAG QTLGSEYDRL 

        70         80         90        100        110        120 
GFLLNLDSKL PAELATKYAN FSEGACKPGY ASALMTAIFP RFSKPAPMFL DDSFRKWARI 

       130        140        150        160        170        180 
REFVPPFGIK GQDNLIKAIL SVTKEYRLTP ALDSLRCRRC IIVGNGGVLA NKSLGSRIDD 

       190        200        210        220        230        240 
YDIVVRLNSA PVKGFEKDVG SKTTLRITYP EGAMQRPEQY ERDSLFVLAG FKWQDFKWLK 

       250        260        270        280        290        300 
YIVYKERVSA SDGFWKSVAT RVPKEPPEIR ILNPYFIQEA AFTLIGLPFN NGLMGRGNIP 

       310        320        330        340        350        360 
TLGSVAVTMA LHGCDEVAVA GFGYDMSTPN APLHYYETVR MAAIKESWTH NIQREKEFLR 

       370 
KLVKARVITD LSSGI 

« Hide

Isoform A1 [UniParc].

Checksum: DCBE59B0BFF74B3A
Show »

FASTA39043,786
Isoform A7 [UniParc].

Checksum: 73BE2801C40F2F9B
Show »

FASTA17019,043
Isoform A8 [UniParc].

Checksum: EDFBE742E527970E
Show »

FASTA44449,649
Isoform B1-90 [UniParc].

Checksum: 0AA0ED4823826782
Show »

FASTA34538,742
Isoform B1+32 [UniParc].

Checksum: 73A783656B89AAF0
Show »

FASTA18921,204
Isoform B3 [UniParc].

Checksum: 9BA97BCA7FA29E8A
Show »

FASTA34438,912
Isoform B4 [UniParc].

Checksum: 7C84EE03A5D6ABCE
Show »

FASTA27731,587
Isoform B4+173 [UniParc].

Checksum: 933010B3A0B41729
Show »

FASTA11512,969
Isoform B5+26 [UniParc].

Checksum: E56B89AAF01B90F8
Show »

FASTA18620,837
Isoform B5+173 [UniParc].

Checksum: 709ABCEF09B26251
Show »

FASTA12113,691
Isoform B7 [UniParc].

Checksum: A881E409E96468F9
Show »

FASTA15517,428
Isoform B8 [UniParc].

Checksum: DF45CA4E6D931B3D
Show »

FASTA42948,034
Isoform B10 [UniParc].

Checksum: 8EF2DF5A045B8511
Show »

FASTA15116,834
Isoform C1 [UniParc].

Checksum: 8A84C7FB0ABDD7C9
Show »

FASTA35940,606
Isoform C4 [UniParc].

Checksum: 3DC939A6817E18B0
Show »

FASTA26130,022
Isoform C5 [UniParc].

Checksum: 1E7D22F363B85B30
Show »

FASTA18620,984
Isoform C7 [UniParc].

Checksum: 04B51A49F74C6F42
Show »

FASTA13915,863
Isoform C8 [UniParc].

Checksum: 1CD13FC0AEB4560D
Show »

FASTA41346,469
Isoform C9 [UniParc].

Checksum: 87D5C4311A1FE514
Show »

FASTA22825,558
Isoform C11 [UniParc].

Checksum: 073EA4B17DC68FB0
Show »

FASTA23026,763
Isoform C12 [UniParc].

Checksum: 33196D8AF2BED686
Show »

FASTA10111,444
Isoform D2+26 [UniParc].

Checksum: C50EA375D4F01821
Show »

FASTA18520,887
Isoform D5 [UniParc].

Checksum: 14056E7DD7DD50AB
Show »

FASTA20122,598
Isoform E1 [UniParc].

Checksum: 9E7CF581E6CD3813
Show »

FASTA435,056
Isoform E3+32 [UniParc].

Checksum: DE5BE566E4BDF07D
Show »

FASTA738,178

References

« Hide 'large scale' references
[1]"Cloning and expression of human Gal beta 1,3(4)GlcNAc alpha 2,3-sialyltransferase."
Kitagawa H., Paulson J.C.
Biochem. Biophys. Res. Commun. 194:375-382(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B1).
Tissue: Placenta.
[2]"Structural variations of the alpha 2,3-sialyltransferase III, ST3GalIII, transcripts in human peripheral white blood cells."
Grahn A., Larson G.
Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A1; A7; A8; B1; B1-90; B1+32; B3; B4; B4+173; B5+26; B5+173; B7; B8; C1; C7; C8; D2+26; E1 AND E3+32).
[3]"Structural variations of the alpha 2,3-sialyltransferase III, ST3GalIII, transcripts in human fetal brain."
Grahn A., Larson G.
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B10; C4; C5; C9; C11; C12 AND D5).
Tissue: Fetal brain.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B1).
Tissue: Brain.
[7]"ST3GAL3 mutations impair the development of higher cognitive functions."
Hu H., Eggers K., Chen W., Garshasbi M., Motazacker M.M., Wrogemann K., Kahrizi K., Tzschach A., Hosseini M., Bahman I., Hucho T., Muhlenhoff M., Gerardy-Schahn R., Najmabadi H., Ropers H.H., Kuss A.W.
Am. J. Hum. Genet. 89:407-414(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MRT12 ASP-13 AND TYR-370, CHARACTERIZATION OF VARIANTS MRT12 ASP-13 AND TYR-370.
[8]"West syndrome caused by ST3Gal-III deficiency."
Edvardson S., Baumann A.M., Muehlenhoff M., Stephan O., Kuss A.W., Shaag A., He L., Zenvirt S., Tanzi R., Gerardy-Schahn R., Elpeleg O.
Epilepsia 54:E24-E27(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EIEE15 PRO-320, CHARACTERIZATION OF VARIANT EIEE15 PRO-320.
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

ST3Gal III

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L23768 mRNA. Translation: AAA35778.1.
AF425851 mRNA. Translation: AAO13859.1.
AF425852 mRNA. Translation: AAO13860.1.
AF425853 mRNA. Translation: AAO13861.1.
AF425854 mRNA. Translation: AAO13862.1.
AF425855 mRNA. Translation: AAO13863.1.
AF425856 mRNA. Translation: AAO13864.1.
AF425857 mRNA. Translation: AAO13865.1.
AF425858 mRNA. Translation: AAO13866.1.
AF425859 mRNA. Translation: AAO13867.1.
AF425860 mRNA. Translation: AAO13868.1.
AF425861 mRNA. Translation: AAO13869.1.
AF425862 mRNA. Translation: AAO13870.1.
AF425863 mRNA. Translation: AAO13871.1.
AF425864 mRNA. Translation: AAO13872.1.
AF425865 mRNA. Translation: AAO13873.1.
AF425866 mRNA. Translation: AAO13874.1.
AF425867 mRNA. Translation: AAO13875.1.
AF425868 mRNA. Translation: AAO13876.1.
AF425869 mRNA. Translation: AAO13877.1.
AY167992 mRNA. Translation: AAO38806.1.
AY167993 mRNA. Translation: AAO38807.1.
AY167994 mRNA. Translation: AAO38808.1.
AY167995 mRNA. Translation: AAO38809.1.
AY167996 mRNA. Translation: AAO38810.1.
AY167997 mRNA. Translation: AAO38811.1.
AY167998 mRNA. Translation: AAO38812.1.
AL451062, AL357079, AL592548 Genomic DNA. Translation: CAH71022.1.
AL451062, AL357079, AL592548 Genomic DNA. Translation: CAH71023.1.
AL451062, AL357079, AL592548 Genomic DNA. Translation: CAH71024.1.
AL451062, AL357079, AL592548 Genomic DNA. Translation: CAH71025.1.
AL451062, AL357079, AL592548 Genomic DNA. Translation: CAH71027.1.
AL451062, AL357079, AL592548 Genomic DNA. Translation: CAH71028.1.
AL451062, AL357079, AL592548 Genomic DNA. Translation: CAH71029.1.
AL451062, AL357079, AL592548 Genomic DNA. Translation: CAH71031.1.
AL451062, AL357079, AL592548 Genomic DNA. Translation: CAH71032.1.
AL451062, AL357079, AL592548 Genomic DNA. Translation: CAH71033.1.
AL357079, AL451062, AL592548 Genomic DNA. Translation: CAI16785.1.
AL357079, AL451062, AL592548 Genomic DNA. Translation: CAI16786.1.
AL357079, AL451062, AL592548 Genomic DNA. Translation: CAI16787.1.
AL357079, AL451062, AL592548 Genomic DNA. Translation: CAI16789.1.
AL357079, AL451062, AL592548 Genomic DNA. Translation: CAI16790.1.
AL357079, AL451062, AL592548 Genomic DNA. Translation: CAI16791.1.
AL357079, AL451062, AL592548 Genomic DNA. Translation: CAI16792.1.
AL357079, AL451062, AL592548 Genomic DNA. Translation: CAI16793.1.
AL357079, AL451062, AL592548 Genomic DNA. Translation: CAI16794.1.
AL357079, AL451062, AL592548 Genomic DNA. Translation: CAI16795.1.
AL592548, AL357079, AL451062 Genomic DNA. Translation: CAI22181.1.
AL592548, AL357079, AL451062 Genomic DNA. Translation: CAI22182.1.
AL592548, AL357079, AL451062 Genomic DNA. Translation: CAI22183.1.
AL592548, AL357079, AL451062 Genomic DNA. Translation: CAI22184.1.
AL592548, AL357079, AL451062 Genomic DNA. Translation: CAI22186.1.
AL592548, AL357079, AL451062 Genomic DNA. Translation: CAI22188.1.
AL592548, AL357079, AL451062 Genomic DNA. Translation: CAI22189.1.
AL592548, AL357079, AL451062 Genomic DNA. Translation: CAI22190.1.
AL592548, AL357079, AL451062 Genomic DNA. Translation: CAI22191.1.
AL592548, AL357079, AL451062 Genomic DNA. Translation: CAI22192.1.
CH471059 Genomic DNA. Translation: EAX07082.1.
CH471059 Genomic DNA. Translation: EAX07083.1.
BC050380 mRNA. Translation: AAH50380.1.
PIRJN0618.
RefSeqNP_001257388.1. NM_001270459.1.
NP_001257389.1. NM_001270460.1.
NP_001257390.1. NM_001270461.1.
NP_001257391.1. NM_001270462.1.
NP_001257392.1. NM_001270463.1.
NP_001257393.1. NM_001270464.1.
NP_001257394.1. NM_001270465.1.
NP_001257395.1. NM_001270466.1.
NP_006270.1. NM_006279.3.
NP_777623.2. NM_174963.3.
NP_777624.1. NM_174964.2.
NP_777625.1. NM_174965.2.
NP_777626.1. NM_174966.2.
NP_777627.1. NM_174967.2.
NP_777628.2. NM_174968.3.
NP_777629.1. NM_174969.2.
NP_777630.1. NM_174970.2.
NP_777631.2. NM_174971.3.
UniGeneHs.597915.

3D structure databases

ProteinModelPortalQ11203.
SMRQ11203. Positions 83-373.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112379. 4 interactions.
IntActQ11203. 5 interactions.
MINTMINT-1397196.

Protein family/group databases

CAZyGT29. Glycosyltransferase Family 29.

PTM databases

PhosphoSiteQ11203.

Polymorphism databases

DMDM1705561.

Proteomic databases

PaxDbQ11203.
PRIDEQ11203.

Protocols and materials databases

DNASU6487.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262915; ENSP00000262915; ENSG00000126091. [Q11203-4]
ENST00000330208; ENSP00000333494; ENSG00000126091. [Q11203-12]
ENST00000332628; ENSP00000329755; ENSG00000126091. [Q11203-7]
ENST00000335430; ENSP00000335633; ENSG00000126091. [Q11203-20]
ENST00000347631; ENSP00000317192; ENSG00000126091. [Q11203-2]
ENST00000351035; ENSP00000316999; ENSG00000126091. [Q11203-19]
ENST00000353126; ENSP00000330463; ENSG00000126091. [Q11203-8]
ENST00000361392; ENSP00000355341; ENSG00000126091. [Q11203-1]
ENST00000361400; ENSP00000354748; ENSG00000126091. [Q11203-15]
ENST00000361746; ENSP00000354657; ENSG00000126091. [Q11203-4]
ENST00000361812; ENSP00000355201; ENSG00000126091. [Q11203-3]
ENST00000372362; ENSP00000361437; ENSG00000126091. [Q11203-12]
ENST00000372365; ENSP00000361440; ENSG00000126091. [Q11203-10]
ENST00000372366; ENSP00000361441; ENSG00000126091. [Q11203-23]
ENST00000372367; ENSP00000361442; ENSG00000126091. [Q11203-24]
ENST00000372368; ENSP00000361443; ENSG00000126091. [Q11203-13]
ENST00000372369; ENSP00000361444; ENSG00000126091. [Q11203-5]
ENST00000372372; ENSP00000361447; ENSG00000126091. [Q11203-19]
ENST00000372374; ENSP00000361449; ENSG00000126091. [Q11203-7]
ENST00000372375; ENSP00000361450; ENSG00000126091. [Q11203-13]
ENST00000372377; ENSP00000361452; ENSG00000126091. [Q11203-14]
ENST00000469715; ENSP00000431700; ENSG00000126091. [Q11203-6]
ENST00000489897; ENSP00000437206; ENSG00000126091. [Q11203-11]
ENST00000490541; ENSP00000435018; ENSG00000126091. [Q11203-26]
ENST00000528371; ENSP00000434876; ENSG00000126091. [Q11203-17]
ENST00000530581; ENSP00000437293; ENSG00000126091. [Q11203-20]
ENST00000531451; ENSP00000435603; ENSG00000126091. [Q11203-18]
ENST00000531816; ENSP00000434378; ENSG00000126091. [Q11203-22]
ENST00000531993; ENSP00000432682; ENSG00000126091. [Q11203-16]
ENST00000533212; ENSP00000435621; ENSG00000126091. [Q11203-14]
ENST00000533933; ENSP00000432965; ENSG00000126091. [Q11203-8]
ENST00000533997; ENSP00000432071; ENSG00000126091. [Q11203-9]
ENST00000545417; ENSP00000439634; ENSG00000126091. [Q11203-3]
GeneID6487.
KEGGhsa:6487.
UCSCuc001cka.4. human. [Q11203-18]
uc001ckb.4. human. [Q11203-4]
uc001ckc.4. human. [Q11203-1]
uc001ckd.4. human. [Q11203-13]
uc001cke.4. human. [Q11203-15]
uc001ckf.4. human. [Q11203-19]
uc001ckg.4. human. [Q11203-8]
uc001cki.4. human. [Q11203-12]
uc001ckk.4. human. [Q11203-7]
uc001ckl.4. human. [Q11203-10]
uc001ckm.4. human. [Q11203-23]
uc001cko.4. human. [Q11203-16]
uc001ckp.4. human. [Q11203-24]
uc001ckq.4. human. [Q11203-17]
uc001ckr.4. human. [Q11203-21]
uc009vwv.4. human. [Q11203-5]
uc009vxb.4. human. [Q11203-22]

Organism-specific databases

CTD6487.
GeneCardsGC01P044173.
HGNCHGNC:10866. ST3GAL3.
HPAHPA051102.
MIM606494. gene.
611090. phenotype.
615006. phenotype.
neXtProtNX_Q11203.
Orphanet88616. Autosomal recessive nonsyndromic intellectual deficit.
3451. West syndrome.
PharmGKBPA35768.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG257001.
HOVERGENHBG056676.
KOK00781.
OMALSCKRCI.
PhylomeDBQ11203.
TreeFamTF354325.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ11203.
BgeeQ11203.
GenevestigatorQ11203.

Family and domain databases

InterProIPR001675. Glyco_trans_29.
IPR012163. Sialyl_trans.
[Graphical view]
PfamPF00777. Glyco_transf_29. 1 hit.
[Graphical view]
PIRSFPIRSF005557. Sialyl_trans. 1 hit.
ProtoNetSearch...

Other

ChiTaRSST3GAL3. human.
GeneWikiST3GAL3.
GenomeRNAi6487.
NextBio25195.
PROQ11203.
SOURCESearch...

Entry information

Entry nameSIAT6_HUMAN
AccessionPrimary (citable) accession number: Q11203
Secondary accession number(s): A9Z1W2 expand/collapse secondary AC list , D3DPX8, Q5T4W9, Q5T4X0, Q5T4X7, Q5T4X8, Q5T4X9, Q5T4Y0, Q5T4Y2, Q5T4Y3, Q5T4Y4, Q86UR6, Q86UR7, Q86UR8, Q86UR9, Q86US0, Q86US1, Q86US2, Q8IX41, Q8IX42, Q8IX43, Q8IX44, Q8IX45, Q8IX46, Q8IX47, Q8IX48, Q8IX49, Q8IX50, Q8IX51, Q8IX52, Q8IX53, Q8IX54, Q8IX55, Q8IX56, Q8IX57, Q8IX58
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM