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Q10471 - GALT2_HUMAN

UniProt

Q10471 - GALT2_HUMAN

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Protein

Polypeptide N-acetylgalactosaminyltransferase 2

Gene

GALNT2

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

Functioni

Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. Probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region.4 Publications

Catalytic activityi

UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.2 Publications

Cofactori

Mn2+2 Publications

Pathwayi

Protein modification; protein glycosylation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei143 – 1431Substrate
Binding sitei176 – 1761Substrate
Binding sitei201 – 2011Substrate
Metal bindingi224 – 2241Manganese1 Publication
Binding sitei225 – 2251Substrate
Metal bindingi226 – 2261Manganese1 Publication
Binding sitei331 – 3311Substrate
Metal bindingi359 – 3591Manganese1 Publication
Binding sitei362 – 3621Substrate
Binding sitei365 – 3651Substrate
Binding sitei367 – 3671Substrate
Sitei516 – 5161Not glycosylated

GO - Molecular functioni

  1. carbohydrate binding Source: UniProtKB-KW
  2. manganese ion binding Source: UniProtKB
  3. polypeptide N-acetylgalactosaminyltransferase activity Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. immunoglobulin biosynthetic process Source: BHF-UCL
  3. O-glycan processing Source: GO_Central
  4. post-translational protein modification Source: Reactome
  5. protein O-linked glycosylation Source: UniProtKB
  6. protein O-linked glycosylation via serine Source: BHF-UCL
  7. protein O-linked glycosylation via threonine Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi2.4.1.41. 2681.
ReactomeiREACT_115606. O-linked glycosylation of mucins.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

Names & Taxonomyi

Protein namesi
Recommended name:
Polypeptide N-acetylgalactosaminyltransferase 2 (EC:2.4.1.41)
Alternative name(s):
Polypeptide GalNAc transferase 2
Short name:
GalNAc-T2
Short name:
pp-GaNTase 2
Protein-UDP acetylgalactosaminyltransferase 2
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2
Cleaved into the following chain:
Polypeptide N-acetylgalactosaminyltransferase 2 soluble form
Gene namesi
Name:GALNT2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:4124. GALNT2.

Subcellular locationi

Golgi apparatus › Golgi stack membrane 1 Publication; Single-pass type II membrane protein 1 Publication. Secreted 1 Publication
Note: Resides preferentially in the trans and medial parts of the Golgi stack. A secreted form also exists.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence Analysis
Transmembranei7 – 2418Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini25 – 571547LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. Golgi apparatus Source: BHF-UCL
  3. Golgi cisterna membrane Source: UniProtKB-SubCell
  4. Golgi membrane Source: Reactome
  5. Golgi stack Source: BHF-UCL
  6. integral component of Golgi membrane Source: BHF-UCL
  7. membrane Source: UniProtKB
  8. perinuclear region of cytoplasm Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28537.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 571571Polypeptide N-acetylgalactosaminyltransferase 2PRO_0000223391Add
BLAST
Chaini52 – 571520Polypeptide N-acetylgalactosaminyltransferase 2 soluble formPRO_0000012265Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi126 ↔ 3541 PublicationPROSITE-ProRule annotation
Disulfide bondi345 ↔ 4231 PublicationPROSITE-ProRule annotation
Disulfide bondi456 ↔ 4731 PublicationPROSITE-ProRule annotation
Disulfide bondi496 ↔ 5131 PublicationPROSITE-ProRule annotation
Disulfide bondi539 ↔ 5551 PublicationPROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ10471.
PaxDbiQ10471.
PeptideAtlasiQ10471.
PRIDEiQ10471.

PTM databases

PhosphoSiteiQ10471.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ10471.
CleanExiHS_GALNT2.
GenevestigatoriQ10471.

Organism-specific databases

HPAiHPA011222.

Interactioni

Protein-protein interaction databases

BioGridi108862. 11 interactions.
MINTiMINT-3026412.
STRINGi9606.ENSP00000355632.

Structurei

Secondary structure

1
571
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi78 – 803Combined sources
Helixi83 – 886Combined sources
Turni98 – 1025Combined sources
Helixi106 – 1116Combined sources
Helixi124 – 1285Combined sources
Beta strandi138 – 1469Combined sources
Helixi149 – 16214Combined sources
Helixi165 – 1673Combined sources
Beta strandi168 – 1758Combined sources
Helixi182 – 1854Combined sources
Helixi186 – 1894Combined sources
Beta strandi193 – 1975Combined sources
Helixi203 – 21412Combined sources
Beta strandi217 – 2226Combined sources
Beta strandi225 – 2295Combined sources
Helixi234 – 24310Combined sources
Beta strandi247 – 25610Combined sources
Turni258 – 2603Combined sources
Beta strandi268 – 2747Combined sources
Beta strandi280 – 2845Combined sources
Helixi287 – 2926Combined sources
Turni293 – 2953Combined sources
Beta strandi308 – 3147Combined sources
Helixi315 – 3206Combined sources
Beta strandi330 – 3334Combined sources
Helixi334 – 34411Combined sources
Beta strandi348 – 35912Combined sources
Turni366 – 3683Combined sources
Helixi373 – 38816Combined sources
Helixi390 – 3923Combined sources
Helixi393 – 3997Combined sources
Helixi401 – 4055Combined sources
Helixi412 – 4209Combined sources
Helixi426 – 4327Combined sources
Beta strandi447 – 4526Combined sources
Beta strandi455 – 4584Combined sources
Turni463 – 4653Combined sources
Beta strandi469 – 4724Combined sources
Helixi478 – 4803Combined sources
Beta strandi482 – 4843Combined sources
Beta strandi490 – 4923Combined sources
Beta strandi495 – 4984Combined sources
Beta strandi509 – 5124Combined sources
Helixi518 – 5203Combined sources
Beta strandi522 – 5254Combined sources
Turni526 – 5294Combined sources
Beta strandi530 – 5334Combined sources
Beta strandi536 – 5416Combined sources
Helixi545 – 5473Combined sources
Beta strandi551 – 5544Combined sources
Helixi559 – 5613Combined sources
Beta strandi564 – 5674Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FFUX-ray1.64A75-571[»]
2FFVX-ray2.75A/B75-571[»]
4D0TX-ray2.45A/B/C/D/E/F1-571[»]
4D0ZX-ray2.20A/B/C/D/E/F1-571[»]
4D11X-ray2.85A/B/C/D/E/F1-571[»]
ProteinModelPortaliQ10471.
SMRiQ10471. Positions 75-568.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ10471.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini443 – 566124Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni135 – 240106Catalytic subdomain AAdd
BLAST
Regioni300 – 36263Catalytic subdomain BAdd
BLAST

Domaini

There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.By similarity
The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.By similarity

Sequence similaritiesi

Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.Curated
Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG239675.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ10471.
KOiK00710.
OMAiGKVRWPD.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ10471.
TreeFamiTF313267.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTiSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q10471-1) [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
MRRRSRMLLC FAFLWVLGIA YYMYSGGGSA LAGGAGGGAG RKEDWNEIDP 
        60         70         80         90        100
IKKKDLHHSN GEEKAQSMET LPPGKVRWPD FNQEAYVGGT MVRSGQDPYA 
       110        120        130        140        150
RNKFNQVESD KLRMDRAIPD TRHDQCQRKQ WRVDLPATSV VITFHNEARS 
       160        170        180        190        200
ALLRTVVSVL KKSPPHLIKE IILVDDYSND PEDGALLGKI EKVRVLRNDR 
       210        220        230        240        250
REGLMRSRVR GADAAQAKVL TFLDSHCECN EHWLEPLLER VAEDRTRVVS 
       260        270        280        290        300
PIIDVINMDN FQYVGASADL KGGFDWNLVF KWDYMTPEQR RSRQGNPVAP 
       310        320        330        340        350
IKTPMIAGGL FVMDKFYFEE LGKYDMMMDV WGGENLEISF RVWQCGGSLE 
       360        370        380        390        400
IIPCSRVGHV FRKQHPYTFP GGSGTVFARN TRRAAEVWMD EYKNFYYAAV 
       410        420        430        440        450
PSARNVPYGN IQSRLELRKK LSCKPFKWYL ENVYPELRVP DHQDIAFGAL 
       460        470        480        490        500
QQGTNCLDTL GHFADGVVGV YECHNAGGNQ EWALTKEKSV KHMDLCLTVV 
       510        520        530        540        550
DRAPGSLIKL QGCRENDSRQ KWEQIEGNSK LRHVGSNLCL DSRTAKSGGL 
       560        570 
SVEVCGPALS QQWKFTLNLQ Q
Length:571
Mass (Da):64,733
Last modified:November 1, 1996 - v1
Checksum:iD9A0F5D17C55BAF2
GO
Isoform 2 (identifier: Q10471-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-90: Missing.
     303-355: TPMIAGGLFV...GGSLEIIPCS → DLVPRVAVWW...HPPGSRGLDG
     356-571: Missing.

Note: No experimental confirmation available.

Show »
Length:265
Mass (Da):30,256
Checksum:i02CD3D8D4652ED95
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti70 – 701T → G AA sequence (PubMed:7592619)Curated
Sequence conflicti78 – 781W → D AA sequence (PubMed:7592619)Curated
Sequence conflicti93 – 931R → G AA sequence (PubMed:7592619)Curated
Sequence conflicti210 – 2101R → W AA sequence (PubMed:7592619)Curated
Sequence conflicti290 – 2912RR → SC AA sequence (PubMed:7592619)Curated
Sequence conflicti293 – 2931R → Q AA sequence (PubMed:7592619)Curated
Sequence conflicti300 – 3001P → H AA sequence (PubMed:7592619)Curated
Sequence conflicti522 – 5221W → A AA sequence (PubMed:7592619)Curated
Sequence conflicti533 – 5331H → M AA sequence (PubMed:7592619)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti245 – 2451R → H.
Corresponds to variant rs1923950 [ dbSNP | Ensembl ].		VAR_049240
Natural varianti554 – 5541V → M.1 Publication
Corresponds to variant rs2273970 [ dbSNP | Ensembl ].		VAR_019575

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9090Missing in isoform 2. 1 PublicationVSP_056491Add
BLAST
Alternative sequencei303 – 35553TPMIA…IIPCS → DLVPRVAVWWQPGDHPVQPC GTRVPEAAPLHVPGWQWHCL CPKHPPGSRGLDG in isoform 2. 1 PublicationVSP_056492Add
BLAST
Alternative sequencei356 – 571216Missing in isoform 2. 1 PublicationVSP_056493Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85019 mRNA. Translation: CAA59381.1.
AK290048 mRNA. Translation: BAF82737.1.
AK304029 mRNA. Translation: BAH14094.1.
AL592228 Genomic DNA. No translation available.
AL078646, AL117349, AL136988 Genomic DNA. Translation: CAC00585.2.
AL117349, AL078646, AL136988 Genomic DNA. Translation: CAI22902.1.
AL136988, AL078646, AL117349 Genomic DNA. Translation: CAI23447.1.
FJ515852 Genomic DNA. Translation: ACS13744.1.
CH471098 Genomic DNA. Translation: EAW69911.1.
BC041120 mRNA. Translation: AAH41120.1.
CCDSiCCDS1582.1. [Q10471-1]
PIRiI37405.
RefSeqiNP_001278795.1. NM_001291866.1.
NP_004472.1. NM_004481.4. [Q10471-1]
UniGeneiHs.743964.

Genome annotation databases

EnsembliENST00000366672; ENSP00000355632; ENSG00000143641. [Q10471-1]
GeneIDi2590.
KEGGihsa:2590.
UCSCiuc010pwa.1. human. [Q10471-1]

Polymorphism databases

DMDMi51315838.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85019 mRNA. Translation: CAA59381.1.
AK290048 mRNA. Translation: BAF82737.1.
AK304029 mRNA. Translation: BAH14094.1.
AL592228 Genomic DNA. No translation available.
AL078646, AL117349, AL136988 Genomic DNA. Translation: CAC00585.2.
AL117349, AL078646, AL136988 Genomic DNA. Translation: CAI22902.1.
AL136988, AL078646, AL117349 Genomic DNA. Translation: CAI23447.1.
FJ515852 Genomic DNA. Translation: ACS13744.1.
CH471098 Genomic DNA. Translation: EAW69911.1.
BC041120 mRNA. Translation: AAH41120.1.
CCDSiCCDS1582.1. [Q10471-1]
PIRiI37405.
RefSeqiNP_001278795.1. NM_001291866.1.
NP_004472.1. NM_004481.4. [Q10471-1]
UniGeneiHs.743964.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FFUX-ray1.64A75-571[»]
2FFVX-ray2.75A/B75-571[»]
4D0TX-ray2.45A/B/C/D/E/F1-571[»]
4D0ZX-ray2.20A/B/C/D/E/F1-571[»]
4D11X-ray2.85A/B/C/D/E/F1-571[»]
ProteinModelPortaliQ10471.
SMRiQ10471. Positions 75-568.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108862. 11 interactions.
MINTiMINT-3026412.
STRINGi9606.ENSP00000355632.

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

PTM databases

PhosphoSiteiQ10471.

Polymorphism databases

DMDMi51315838.

Proteomic databases

MaxQBiQ10471.
PaxDbiQ10471.
PeptideAtlasiQ10471.
PRIDEiQ10471.

Protocols and materials databases

DNASUi2590.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366672; ENSP00000355632; ENSG00000143641. [Q10471-1]
GeneIDi2590.
KEGGihsa:2590.
UCSCiuc010pwa.1. human. [Q10471-1]

Organism-specific databases

CTDi2590.
GeneCardsiGC01P230193.
H-InvDBHIX0001682.
HGNCiHGNC:4124. GALNT2.
HPAiHPA011222.
MIMi602274. gene.
neXtProtiNX_Q10471.
PharmGKBiPA28537.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG239675.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ10471.
KOiK00710.
OMAiGKVRWPD.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ10471.
TreeFamiTF313267.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.1.41. 2681.
ReactomeiREACT_115606. O-linked glycosylation of mucins.

Miscellaneous databases

ChiTaRSiGALNT2. human.
EvolutionaryTraceiQ10471.
GeneWikiiGALNT2.
GenomeRNAii2590.
NextBioi10245.
PROiQ10471.
SOURCEiSearch...

Gene expression databases

BgeeiQ10471.
CleanExiHS_GALNT2.
GenevestigatoriQ10471.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTiSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase."
    White T., Bennett E.P., Takio K., Soerensen T., Bonding N., Clausen H.
    J. Biol. Chem. 270:24156-24165(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 52-93; 104-120; 170-182; 193-218; 303-323; 421-424 AND 510-546, FUNCTION, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
    Tissue: Gastric carcinoma.
  2. "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 2), VARIANT MET-554.
    Tissue: Hippocampus and Trachea.
  3. "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].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. NHLBI resequencing and genotyping service (RS&G)
    Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [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 1).
    Tissue: Lymph.
  7. "Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3."
    Wandall H.H., Hassan H., Mirgorodskaya E., Kristensen A.K., Roepstorff P., Bennett E.P., Nielsen P.A., Hollingsworth M.A., Burchell J., Taylor-Papadimitriou J., Clausen H.
    J. Biol. Chem. 272:23503-23514(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus."
    Roettger S., White J., Wandall H.H., Olivo J.-C., Stark A., Bennett E.P., Whitehouse C., Berger E.G., Clausen H., Nilsson T.
    J. Cell Sci. 111:45-60(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "Initiation of O-glycan synthesis in IgA1 hinge region is determined by a single enzyme, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2."
    Iwasaki H., Zhang Y., Tachibana K., Gotoh M., Kikuchi N., Kwon Y.-D., Togayachi A., Kudo T., Kubota T., Narimatsu H.
    J. Biol. Chem. 278:5613-5621(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Dynamic association between the catalytic and lectin domains of human UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-2."
    Fritz T.A., Raman J., Tabak L.A.
    J. Biol. Chem. 281:8613-8619(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 75-571 IN COMPLEX WITH UDP; PEPTIDE SUBSTRATE AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DISULFIDE BONDS.
+Additional computationally mapped references.

Entry informationi

Entry nameiGALT2_HUMAN
AccessioniPrimary (citable) accession number: Q10471
Secondary accession number(s): A8K1Y3
, B7Z8V8, C5HU00, Q9NPY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: November 1, 1996
Last modified: February 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

3D-structure, Complete proteome, Direct protein sequencing, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.