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Protein

N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2

Gene

B3GNT2

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

Functioni

Beta-1,3-N-acetylglucosaminyltransferase involved in the synthesis of poly-N-acetyllactosamine. Catalyzes the initiation and elongation of poly-N-acetyllactosamine chains. Shows a marked preference for Gal(beta1-4)Glc(NAc)-based acceptors (PubMed:9892646). Probably constitutes the main polylactosamine synthase.3 Publications

Catalytic activityi

UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminyl-R.3 Publications

Cofactori

Mn2+1 Publication

Pathway: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.1 Publication
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese

Enzyme and pathway databases

ReactomeiREACT_115606. O-linked glycosylation of mucins.
REACT_121120. Keratan sulfate biosynthesis.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2 (EC:2.4.1.1493 Publications)
Alternative name(s):
Beta-1,3-N-acetylglucosaminyltransferase 1
Short name:
BGnT-1
Short name:
Beta-1,3-Gn-T1
Short name:
Beta3Gn-T1
Beta-1,3-galactosyltransferase 7
Short name:
Beta-1,3-GalTase 7
Short name:
Beta3Gal-T7
Short name:
Beta3GalT7
Short name:
b3Gal-T7
Beta-3-Gx-T7
UDP-Gal:beta-GlcNAc beta-1,3-galactosyltransferase 7
UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2
Short name:
BGnT-2
Short name:
Beta-1,3-Gn-T2
Short name:
Beta-1,3-N-acetylglucosaminyltransferase 2
Short name:
Beta3Gn-T2
UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase 7
Gene namesi
Name:B3GNT2
Synonyms:B3GALT7, B3GNT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:15629. B3GNT2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 77CytoplasmicSequence Analysis
Transmembranei8 – 2821Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini29 – 397369LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • Golgi membrane Source: Reactome
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi245 – 2451D → A: Loss of enzymatic activity, no loss of B3GNT8-binding. 1 Publication

Organism-specific databases

PharmGKBiPA25218.

Polymorphism and mutation databases

BioMutaiB3GNT2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 397397N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2PRO_0000219170Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi79 – 791N-linked (GlcNAc...)1 Publication
Glycosylationi89 – 891N-linked (GlcNAc...)Sequence Analysis
Glycosylationi127 – 1271N-linked (GlcNAc...)Sequence Analysis
Glycosylationi173 – 1731N-linked (GlcNAc...)Sequence Analysis
Glycosylationi219 – 2191N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9NY97.
PaxDbiQ9NY97.
PRIDEiQ9NY97.

PTM databases

PhosphoSiteiQ9NY97.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ9NY97.
CleanExiHS_B3GNT1.
HS_B3GNT2.
GenevisibleiQ9NY97. HS.

Organism-specific databases

HPAiHPA005997.

Interactioni

Subunit structurei

Interacts with B3GNT8; this interaction greatly increases B3GNT2 catalytic activity, independently of B3GNT8 enzymatic activity.1 Publication

Protein-protein interaction databases

BioGridi115919. 18 interactions.
IntActiQ9NY97. 1 interaction.
STRINGi9606.ENSP00000305595.

Structurei

3D structure databases

ProteinModelPortaliQ9NY97.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 31 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG262849.
GeneTreeiENSGT00760000118879.
HOGENOMiHOG000232195.
HOVERGENiHBG050653.
InParanoidiQ9NY97.
KOiK00741.
OMAiIDIWSRL.
OrthoDBiEOG7BGHKT.
PhylomeDBiQ9NY97.
TreeFamiTF318639.

Family and domain databases

InterProiIPR002659. Glyco_trans_31.
[Graphical view]
PANTHERiPTHR11214. PTHR11214. 1 hit.
PfamiPF01762. Galactosyl_T. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NY97-1) [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
MSVGRRRIKL LGILMMANVF IYFIMEVSKS SSQEKNGKGE VIIPKEKFWK
60 70 80 90 100
ISTPPEAYWN REQEKLNRQY NPILSMLTNQ TGEAGRLSNI SHLNYCEPDL
110 120 130 140 150
RVTSVVTGFN NLPDRFKDFL LYLRCRNYSL LIDQPDKCAK KPFLLLAIKS
160 170 180 190 200
LTPHFARRQA IRESWGQESN AGNQTVVRVF LLGQTPPEDN HPDLSDMLKF
210 220 230 240 250
ESEKHQDILM WNYRDTFFNL SLKEVLFLRW VSTSCPDTEF VFKGDDDVFV
260 270 280 290 300
NTHHILNYLN SLSKTKAKDL FIGDVIHNAG PHRDKKLKYY IPEVVYSGLY
310 320 330 340 350
PPYAGGGGFL YSGHLALRLY HITDQVHLYP IDDVYTGMCL QKLGLVPEKH
360 370 380 390
KGFRTFDIEE KNKNNICSYV DLMLVHSRKP QEMIDIWSQL QSAHLKC
Length:397
Mass (Da):46,022
Last modified:April 11, 2003 - v2
Checksum:iB104ECCAE26DC4AC
GO
Isoform 2 (identifier: Q9NY97-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: MSVGRRRIKLL → MVSRSLV

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.
Show »
Length:393
Mass (Da):45,484
Checksum:iDA6ECD0416167FEF
GO

Sequence cautioni

The sequence BAA92031.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111L → LL in CAB91546 (Ref. 3) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1111MSVGRRRIKLL → MVSRSLV in isoform 2. 1 PublicationVSP_001791Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF092051 mRNA. Translation: AAD09764.2.
AJ006077 mRNA. Translation: CAB91546.1.
AF288208 mRNA. Translation: AAF97253.1.
AF288209 mRNA. Translation: AAF97254.1.
AB049584 mRNA. Translation: BAB21530.1.
BC030579 mRNA. Translation: AAH30579.1.
AC093401 Genomic DNA. Translation: AAX93271.1.
CH471053 Genomic DNA. Translation: EAW99977.1.
CH471053 Genomic DNA. Translation: EAW99978.1.
CH471053 Genomic DNA. Translation: EAW99979.1.
BC047933 mRNA. Translation: AAH47933.1.
AK002009 mRNA. Translation: BAA92031.1. Different initiation.
CCDSiCCDS1870.1. [Q9NY97-1]
RefSeqiNP_006568.2. NM_006577.5. [Q9NY97-1]
UniGeneiHs.173203.

Genome annotation databases

EnsembliENST00000301998; ENSP00000305595; ENSG00000170340. [Q9NY97-1]
ENST00000405767; ENSP00000384692; ENSG00000170340. [Q9NY97-1]
GeneIDi10678.
KEGGihsa:10678.
UCSCiuc002sbs.3. human. [Q9NY97-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF092051 mRNA. Translation: AAD09764.2.
AJ006077 mRNA. Translation: CAB91546.1.
AF288208 mRNA. Translation: AAF97253.1.
AF288209 mRNA. Translation: AAF97254.1.
AB049584 mRNA. Translation: BAB21530.1.
BC030579 mRNA. Translation: AAH30579.1.
AC093401 Genomic DNA. Translation: AAX93271.1.
CH471053 Genomic DNA. Translation: EAW99977.1.
CH471053 Genomic DNA. Translation: EAW99978.1.
CH471053 Genomic DNA. Translation: EAW99979.1.
BC047933 mRNA. Translation: AAH47933.1.
AK002009 mRNA. Translation: BAA92031.1. Different initiation.
CCDSiCCDS1870.1. [Q9NY97-1]
RefSeqiNP_006568.2. NM_006577.5. [Q9NY97-1]
UniGeneiHs.173203.

3D structure databases

ProteinModelPortaliQ9NY97.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115919. 18 interactions.
IntActiQ9NY97. 1 interaction.
STRINGi9606.ENSP00000305595.

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

PTM databases

PhosphoSiteiQ9NY97.

Polymorphism and mutation databases

BioMutaiB3GNT2.

Proteomic databases

MaxQBiQ9NY97.
PaxDbiQ9NY97.
PRIDEiQ9NY97.

Protocols and materials databases

DNASUi10678.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000301998; ENSP00000305595; ENSG00000170340. [Q9NY97-1]
ENST00000405767; ENSP00000384692; ENSG00000170340. [Q9NY97-1]
GeneIDi10678.
KEGGihsa:10678.
UCSCiuc002sbs.3. human. [Q9NY97-1]

Organism-specific databases

CTDi10678.
GeneCardsiGC02P062423.
HGNCiHGNC:15629. B3GNT2.
HPAiHPA005997.
MIMi605581. gene.
neXtProtiNX_Q9NY97.
PharmGKBiPA25218.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG262849.
GeneTreeiENSGT00760000118879.
HOGENOMiHOG000232195.
HOVERGENiHBG050653.
InParanoidiQ9NY97.
KOiK00741.
OMAiIDIWSRL.
OrthoDBiEOG7BGHKT.
PhylomeDBiQ9NY97.
TreeFamiTF318639.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiREACT_115606. O-linked glycosylation of mucins.
REACT_121120. Keratan sulfate biosynthesis.

Miscellaneous databases

ChiTaRSiB3GNT2. human.
GeneWikiiB3GNT2.
GenomeRNAii10678.
NextBioi40601.
PROiQ9NY97.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NY97.
CleanExiHS_B3GNT1.
HS_B3GNT2.
GenevisibleiQ9NY97. HS.

Family and domain databases

InterProiIPR002659. Glyco_trans_31.
[Graphical view]
PANTHERiPTHR11214. PTHR11214. 1 hit.
PfamiPF01762. Galactosyl_T. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A beta-1,3-N-acetylglucosaminyltransferase with poly-N-acetyllactosamine synthase activity is structurally related to beta-1,3-galactosyltransferases."
    Zhou D., Dinter A., Gutierrez Gallego R., Kamerling J.P., Vliegenthart J.F.G., Berger E.G., Hennet T.
    Proc. Natl. Acad. Sci. U.S.A. 96:406-411(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, COFACTOR, CATALYTIC ACTIVITY.
    Tissue: Brain.
  2. Zhou D., Berger E.G., Hennet T.
    Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Cloning and expression of two beta-1,3-galactosyltransferases: beta3gal-T5 and beta3gal-T6."
    Amado M., Carneiro F., Clausen H.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "A novel member of beta-1,3-galactosyltransferase family is down regulated during bladder TCC progression."
    Gromova I., Gromov P., Celis J.E.
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Urinary bladder.
  5. "Identification and characterization of three novel beta 1,3-N-acetylglucosaminyltransferases structurally related to the beta 1,3-galactosyltransferase family."
    Shiraishi N., Natsume A., Togayachi A., Endo T., Akashima T., Yamada Y., Imai N., Nakagawa S., Koizumi S., Sekine S., Narimatsu H., Sasaki K.
    J. Biol. Chem. 276:3498-3507(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, TISSUE SPECIFICITY, FUNCTION.
  6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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).
    Tissue: Brain and Testis.
  9. "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] OF 25-397.
    Tissue: Placenta.
  10. "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.
  11. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
  12. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-79.
    Tissue: Plasma.
  13. "Activation of beta1,3-N-acetylglucosaminyltransferase-2 (beta3Gn-T2) by beta3Gn-T8. Possible involvement of beta3Gn-T8 in increasing poly-N-acetyllactosamine chains in differentiated HL-60 cells."
    Seko A., Yamashita K.
    J. Biol. Chem. 283:33094-33100(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH B3GNT8, MUTAGENESIS OF ASP-245.
  14. "B4GAT1 is the priming enzyme for the LARGE-dependent functional glycosylation of alpha-dystroglycan."
    Praissman J.L., Live D.H., Wang S., Ramiah A., Chinoy Z.S., Boons G.J., Moremen K.W., Wells L.
    Elife 3:0-0(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.

Entry informationi

Entry nameiB3GN2_HUMAN
AccessioniPrimary (citable) accession number: Q9NY97
Secondary accession number(s): Q54AC1
, Q9NQQ9, Q9NQR0, Q9NUT9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: April 11, 2003
Last modified: June 24, 2015
This is version 131 of the entry and version 2 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

Caution

Was indicated as B3Gal-T6 in submitted DNA entries.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. 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.