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Protein

Beta-1,4-galactosyltransferase 2

Gene

B4GALT2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. Can produce lactose.

Catalytic activityi

UDP-alpha-D-galactose + D-glucose = UDP + lactose.
UDP-alpha-D-galactose + N-acetyl-beta-D-glucosaminylglycopeptide = UDP + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminylglycopeptide.
UDP-alpha-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine.

Cofactori

Mn2+By similarity

Kineticsi

  1. KM=71 µM for GlcNAc-B-S-pNP1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi218 – 2181ManganeseBy similarity
Binding sitei278 – 2781UDP-alpha-D-galactoseBy similarity
Metal bindingi311 – 3111Manganese; via tele nitrogenBy similarity
Binding sitei323 – 3231N-acetyl-D-glucosamineBy similarity

GO - Molecular functioni

  1. beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity Source: UniProtKB-EC
  2. galactosyltransferase activity Source: ProtInc
  3. lactose synthase activity Source: UniProtKB-EC
  4. metal ion binding Source: UniProtKB-KW
  5. N-acetyllactosamine synthase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. cellular protein metabolic process Source: Reactome
  3. glycosaminoglycan metabolic process Source: Reactome
  4. keratan sulfate biosynthetic process Source: Reactome
  5. keratan sulfate metabolic process Source: Reactome
  6. pathogenesis Source: Reactome
  7. post-translational protein modification Source: Reactome
  8. protein N-linked glycosylation via asparagine Source: Reactome
  9. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_121120. Keratan sulfate biosynthesis.
REACT_25085. N-Glycan antennae elongation.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT7. Glycosyltransferase Family 7.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-1,4-galactosyltransferase 2 (EC:2.4.1.-)
Short name:
Beta-1,4-GalTase 2
Short name:
Beta4Gal-T2
Short name:
b4Gal-T2
Alternative name(s):
UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 2
UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 2
Including the following 4 domains:
Lactose synthase A protein (EC:2.4.1.22)
N-acetyllactosamine synthase (EC:2.4.1.90)
Alternative name(s):
Nal synthase
Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase (EC:2.4.1.38)
Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase (EC:2.4.1.-)
Gene namesi
Name:B4GALT2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:925. B4GALT2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1515CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei16 – 3621Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini37 – 372336LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. Golgi cisterna membrane Source: UniProtKB-SubCell
  2. Golgi membrane Source: Reactome
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25224.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 372372Beta-1,4-galactosyltransferase 2PRO_0000080533Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi66 – 661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi71 – 711N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi97 ↔ 139By similarity
Disulfide bondi211 ↔ 230By similarity
Glycosylationi357 – 3571N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiO60909.
PaxDbiO60909.
PRIDEiO60909.

PTM databases

PhosphoSiteiO60909.

Expressioni

Tissue specificityi

Weakly expressed in various tissues. Highest expression in prostate, testis, ovary, intestine, muscle, and in fetal brain.

Gene expression databases

BgeeiO60909.
CleanExiHS_B4GALT2.
ExpressionAtlasiO60909. baseline and differential.
GenevestigatoriO60909.

Organism-specific databases

HPAiHPA047739.

Interactioni

Protein-protein interaction databases

BioGridi114247. 1 interaction.
IntActiO60909. 1 interaction.
STRINGi9606.ENSP00000349293.

Structurei

3D structure databases

ProteinModelPortaliO60909.
SMRiO60909. Positions 97-365.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni150 – 1545UDP-alpha-D-galactose bindingBy similarity
Regioni189 – 1913UDP-alpha-D-galactose bindingBy similarity
Regioni217 – 2182UDP-alpha-D-galactose bindingBy similarity
Regioni280 – 2834N-acetyl-D-glucosamine bindingBy similarity
Regioni311 – 3133UDP-alpha-D-galactose bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyltransferase 7 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG327897.
GeneTreeiENSGT00760000119140.
HOGENOMiHOG000231027.
HOVERGENiHBG058334.
InParanoidiO60909.
KOiK07967.
OMAiEQPRHFA.
OrthoDBiEOG7060R0.
PhylomeDBiO60909.
TreeFamiTF312834.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR003859. Galactosyl_T.
IPR027791. Galactosyl_T_C.
IPR027995. Galactosyl_T_N.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR19300. PTHR19300. 1 hit.
PfamiPF02709. Glyco_transf_7C. 1 hit.
PF13733. Glyco_transf_7N. 1 hit.
[Graphical view]
PRINTSiPR02050. B14GALTRFASE.
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O60909-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSRLLGGTLE RVCKAVLLLC LLHFLVAVIL YFDVYAQHLA FFSRFSARGP
60 70 80 90 100
AHALHPAASS SSSSSNCSRP NATASSSGLP EVPSALPGPT APTLPPCPDS
110 120 130 140 150
PPGLVGRLLI EFTSPMPLER VQRENPGVLM GGRYTPPDCT PAQTVAVIIP
160 170 180 190 200
FRHREHHLRY WLHYLHPILR RQRLRYGVYV INQHGEDTFN RAKLLNVGFL
210 220 230 240 250
EALKEDAAYD CFIFSDVDLV PMDDRNLYRC GDQPRHFAIA MDKFGFRLPY
260 270 280 290 300
AGYFGGVSGL SKAQFLRING FPNEYWGWGG EDDDIFNRIS LTGMKISRPD
310 320 330 340 350
IRIGRYRMIK HDRDKHNEPN PQRFTKIQNT KLTMKRDGIG SVRYQVLEVS
360 370
RQPLFTNITV DIGRPPSWPP RG
Length:372
Mass (Da):41,972
Last modified:August 1, 1998 - v1
Checksum:iA6F7800251AA1E4F
GO
Isoform 2 (identifier: O60909-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-118: Missing.
     119-119: E → MPSTQLLAAAAAAATAPGPTPPPLAPGSLRSPVPCPVPRLPRCHPVLTRHLVL

Note: No experimental confirmation available.

Show »
Length:306
Mass (Da):34,883
Checksum:iA483868104528A2B
GO
Isoform 3 (identifier: O60909-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAVEVQEQWPCLPAAGCPGPLGGPVAACGM

Note: No experimental confirmation available.

Show »
Length:401
Mass (Da):44,764
Checksum:i70B4877C779850C1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti100 – 1001S → TS (PubMed:9597550).Curated
Sequence conflicti136 – 1361P → S in AAC39733 (PubMed:9597550).Curated
Sequence conflicti177 – 1771G → C in AAC39733 (PubMed:9597550).Curated
Sequence conflicti315 – 3162KH → ND in AAC39733 (PubMed:9597550).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti122 – 1221Q → H.1 Publication
Corresponds to variant rs1859728 [ dbSNP | Ensembl ].
VAR_020487
Natural varianti338 – 3381G → R.
Corresponds to variant rs35904809 [ dbSNP | Ensembl ].
VAR_054021

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 118118Missing in isoform 2. CuratedVSP_014103Add
BLAST
Alternative sequencei1 – 11M → MAVEVQEQWPCLPAAGCPGP LGGPVAACGM in isoform 3. 1 PublicationVSP_043010
Alternative sequencei119 – 1191E → MPSTQLLAAAAAAATAPGPT PPPLAPGSLRSPVPCPVPRL PRCHPVLTRHLVL in isoform 2. CuratedVSP_014104

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12510 mRNA. Translation: CAA73112.1.
AF038660 mRNA. Translation: AAC39733.1.
AB024434 mRNA. Translation: BAA75819.1.
AK095873 mRNA. Translation: BAG53152.1.
AK293418 mRNA. Translation: BAG56925.1.
AL139220, AL357079 Genomic DNA. Translation: CAI19431.1.
AL139220, AL357079 Genomic DNA. Translation: CAI19432.1.
AL357079, AL139220 Genomic DNA. Translation: CAI16802.1.
AL357079, AL139220 Genomic DNA. Translation: CAI16803.1.
CH471059 Genomic DNA. Translation: EAX07062.1.
CH471059 Genomic DNA. Translation: EAX07063.1.
CH471059 Genomic DNA. Translation: EAX07064.1.
CH471059 Genomic DNA. Translation: EAX07065.1.
BC096821 mRNA. Translation: AAH96821.1.
AL137647 mRNA. Translation: CAB70857.1.
CCDSiCCDS506.1. [O60909-1]
CCDS55596.1. [O60909-3]
PIRiT46511.
RefSeqiNP_001005417.1. NM_001005417.2. [O60909-1]
NP_003771.1. NM_003780.4. [O60909-1]
NP_085076.2. NM_030587.2. [O60909-3]
XP_005271361.1. XM_005271304.2. [O60909-1]
XP_006711080.1. XM_006711017.1. [O60909-1]
UniGeneiHs.632403.
Hs.736507.

Genome annotation databases

EnsembliENST00000309519; ENSP00000310696; ENSG00000117411. [O60909-3]
ENST00000356836; ENSP00000349293; ENSG00000117411. [O60909-1]
ENST00000372324; ENSP00000361399; ENSG00000117411. [O60909-1]
ENST00000434555; ENSP00000407468; ENSG00000117411. [O60909-2]
GeneIDi8704.
KEGGihsa:8704.
UCSCiuc001clg.3. human. [O60909-1]
uc001clh.3. human. [O60909-2]
uc010okl.2. human. [O60909-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Beta-1,4-galactosyltransferase 2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12510 mRNA. Translation: CAA73112.1.
AF038660 mRNA. Translation: AAC39733.1.
AB024434 mRNA. Translation: BAA75819.1.
AK095873 mRNA. Translation: BAG53152.1.
AK293418 mRNA. Translation: BAG56925.1.
AL139220, AL357079 Genomic DNA. Translation: CAI19431.1.
AL139220, AL357079 Genomic DNA. Translation: CAI19432.1.
AL357079, AL139220 Genomic DNA. Translation: CAI16802.1.
AL357079, AL139220 Genomic DNA. Translation: CAI16803.1.
CH471059 Genomic DNA. Translation: EAX07062.1.
CH471059 Genomic DNA. Translation: EAX07063.1.
CH471059 Genomic DNA. Translation: EAX07064.1.
CH471059 Genomic DNA. Translation: EAX07065.1.
BC096821 mRNA. Translation: AAH96821.1.
AL137647 mRNA. Translation: CAB70857.1.
CCDSiCCDS506.1. [O60909-1]
CCDS55596.1. [O60909-3]
PIRiT46511.
RefSeqiNP_001005417.1. NM_001005417.2. [O60909-1]
NP_003771.1. NM_003780.4. [O60909-1]
NP_085076.2. NM_030587.2. [O60909-3]
XP_005271361.1. XM_005271304.2. [O60909-1]
XP_006711080.1. XM_006711017.1. [O60909-1]
UniGeneiHs.632403.
Hs.736507.

3D structure databases

ProteinModelPortaliO60909.
SMRiO60909. Positions 97-365.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114247. 1 interaction.
IntActiO60909. 1 interaction.
STRINGi9606.ENSP00000349293.

Chemistry

DrugBankiDB00141. N-Acetyl-D-glucosamine.

Protein family/group databases

CAZyiGT7. Glycosyltransferase Family 7.

PTM databases

PhosphoSiteiO60909.

Proteomic databases

MaxQBiO60909.
PaxDbiO60909.
PRIDEiO60909.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000309519; ENSP00000310696; ENSG00000117411. [O60909-3]
ENST00000356836; ENSP00000349293; ENSG00000117411. [O60909-1]
ENST00000372324; ENSP00000361399; ENSG00000117411. [O60909-1]
ENST00000434555; ENSP00000407468; ENSG00000117411. [O60909-2]
GeneIDi8704.
KEGGihsa:8704.
UCSCiuc001clg.3. human. [O60909-1]
uc001clh.3. human. [O60909-2]
uc010okl.2. human. [O60909-3]

Organism-specific databases

CTDi8704.
GeneCardsiGC01P044444.
HGNCiHGNC:925. B4GALT2.
HPAiHPA047739.
MIMi604013. gene.
neXtProtiNX_O60909.
PharmGKBiPA25224.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG327897.
GeneTreeiENSGT00760000119140.
HOGENOMiHOG000231027.
HOVERGENiHBG058334.
InParanoidiO60909.
KOiK07967.
OMAiEQPRHFA.
OrthoDBiEOG7060R0.
PhylomeDBiO60909.
TreeFamiTF312834.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiREACT_121120. Keratan sulfate biosynthesis.
REACT_25085. N-Glycan antennae elongation.

Miscellaneous databases

ChiTaRSiB4GALT2. human.
GeneWikiiB4GALT2.
GenomeRNAii8704.
NextBioi32635.
PROiO60909.
SOURCEiSearch...

Gene expression databases

BgeeiO60909.
CleanExiHS_B4GALT2.
ExpressionAtlasiO60909. baseline and differential.
GenevestigatoriO60909.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR003859. Galactosyl_T.
IPR027791. Galactosyl_T_C.
IPR027995. Galactosyl_T_N.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR19300. PTHR19300. 1 hit.
PfamiPF02709. Glyco_transf_7C. 1 hit.
PF13733. Glyco_transf_7N. 1 hit.
[Graphical view]
PRINTSiPR02050. B14GALTRFASE.
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A family of human beta4-galactosyltransferases. Cloning and expression of two novel UDP-galactose:beta-n-acetylglucosamine beta1, 4-galactosyltransferases, beta4Gal-T2 and beta4Gal-T3."
    Almeida R., Amado M., David L., Levery S.B., Holmes E.H., Merkx G., van Kessel A.G., Rygaard E., Hassan H., Bennett E., Clausen H.
    J. Biol. Chem. 272:31979-31991(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "The expanding beta 4-galactosyltransferase gene family: messages from the databanks."
    Lo N.-W., Shaper J.H., Pevsner J., Shaper N.L.
    Glycobiology 8:517-526(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells."
    Guo S., Sato T., Shirane K., Furukawa K.
    Glycobiology 11:813-820(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), BIOPHYSICOCHEMICAL PROPERTIES.
    Tissue: Erythroleukemia.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
  5. "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.
    , 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].
  6. 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] (ISOFORM 1), VARIANT HIS-122.
    Tissue: Chondrosarcoma.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 149-372 (ISOFORMS 1/2).
    Tissue: Uterus.
  9. "Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions."
    Amado M., Almeida R., Schwientek T., Clausen H.
    Biochim. Biophys. Acta 1473:35-53(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiB4GT2_HUMAN
AccessioniPrimary (citable) accession number: O60909
Secondary accession number(s): B3KTP0
, B4DE14, D3DPY6, D3DPY7, O60511, Q4V9L9, Q5T4X5, Q5T4Y5, Q9BUP6, Q9NSY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: August 1, 1998
Last modified: March 4, 2015
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.