Q10471 (GALT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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:

1. Polypeptide N-acetylgalactosaminyltransferase 2 soluble form

Gene names

Name:

GALNT2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	571 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 Ref.7 Ref.9 Ref.12
Catalytic activity	UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide. Ref.1 Ref.12
Cofactor	Manganese. Ref.1 Ref.12
Pathway	Protein modification; protein glycosylation.
Subcellular location	Golgi apparatus › Golgi stack membrane; Single-pass type II membrane protein. Secreted. Note: Resides preferentially in the trans and medial parts of the Golgi stack. A secreted form also exists. Ref.8
Tissue specificity	Widely expressed. Ref.1
Domain	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 similarities	Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily. Contains 1 ricin B-type lectin domain.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane Secreted
Coding sequence diversity	Polymorphism
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Lectin Manganese Metal-binding
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	O-glycan processing Traceable author statement. Source: Reactome immunoglobulin biosynthetic process Inferred from direct assay Ref.9. Source: BHF-UCL post-translational protein modification Traceable author statement. Source: Reactome protein O-linked glycosylation via serine Inferred from direct assay Ref.9Ref.7. Source: BHF-UCL protein O-linked glycosylation via threonine Inferred from direct assay Ref.9Ref.7. Source: BHF-UCL
Cellular_component	Golgi cisterna membrane Inferred from electronic annotation. Source: UniProtKB-SubCell Golgi stack Inferred from direct assay PubMed 9852147. Source: BHF-UCL extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral component of Golgi membrane Non-traceable author statement PubMed 9852147. Source: BHF-UCL perinuclear region of cytoplasm Inferred from direct assay PubMed 12506059. Source: BHF-UCL
Molecular_function	manganese ion binding Inferred from direct assay Ref.12. Source: UniProtKB polypeptide N-acetylgalactosaminyltransferase activity Inferred from direct assay Ref.12. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 571

571

Polypeptide N-acetylgalactosaminyltransferase 2

PRO_0000223391

Chain

52 – 571

520

Polypeptide N-acetylgalactosaminyltransferase 2 soluble form

PRO_0000012265

Regions

Topological domain

1 – 6

6

Cytoplasmic Potential

Transmembrane

7 – 24

18

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

25 – 571

547

Lumenal Potential

Domain

443 – 566

124

Ricin B-type lectin

Region

135 – 240

106

Catalytic subdomain A

Region

300 – 362

63

Catalytic subdomain B

Sites

Metal binding

224

1

Manganese

Metal binding

226

1

Manganese

Metal binding

359

1

Manganese

Binding site

143

1

Substrate

Binding site

176

1

Substrate

Binding site

201

1

Substrate

Binding site

225

1

Substrate

Binding site

331

1

Substrate

Binding site

362

1

Substrate

Binding site

365

1

Substrate

Binding site

367

1

Substrate

Site

516

1

Not glycosylated

Amino acid modifications

Disulfide bond

126 ↔ 354

Ref.12

Disulfide bond

345 ↔ 423

Ref.12

Disulfide bond

456 ↔ 473

Ref.12

Disulfide bond

496 ↔ 513

Ref.12

Disulfide bond

539 ↔ 555

Ref.12

Natural variations

Natural variant

245

1

R → H.
Corresponds to variant rs1923950 [ dbSNP | Ensembl ].

VAR_049240

Natural variant

554

1

V → M. Ref.2
Corresponds to variant rs2273970 [ dbSNP | Ensembl ].

VAR_019575

Experimental info

Sequence conflict

70

1

T → G AA sequence Ref.1

Sequence conflict

78

1

W → D AA sequence Ref.1

Sequence conflict

93

1

R → G AA sequence Ref.1

Sequence conflict

210

1

R → W AA sequence Ref.1

Sequence conflict

290 – 291

2

RR → SC AA sequence Ref.1

Sequence conflict

293

1

R → Q AA sequence Ref.1

Sequence conflict

300

1

P → H AA sequence Ref.1

Sequence conflict

522

1

W → A AA sequence Ref.1

Sequence conflict

533

1

H → M AA sequence Ref.1

Secondary structure

1

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571

Helix Strand Turn

Details...

Helix

78 – 80

3

Helix

83 – 88

6

Turn

98 – 102

5

Helix

106 – 111

6

Helix

124 – 128

5

Beta strand

138 – 146

9

Helix

149 – 162

14

Helix

165 – 167

3

Beta strand

168 – 175

8

Helix

182 – 185

4

Helix

186 – 189

4

Beta strand

193 – 197

5

Helix

203 – 214

12

Beta strand

217 – 222

6

Beta strand

225 – 229

5

Helix

234 – 243

10

Beta strand

247 – 256

10

Turn

258 – 260

3

Beta strand

268 – 274

7

Beta strand

280 – 284

5

Helix

287 – 292

6

Beta strand

308 – 314

7

Helix

315 – 320

6

Beta strand

330 – 333

4

Helix

334 – 344

11

Beta strand

348 – 359

12

Turn

366 – 368

3

Helix

373 – 388

16

Helix

390 – 392

3

Helix

393 – 399

7

Helix

401 – 405

5

Helix

412 – 420

9

Helix

426 – 432

7

Beta strand

447 – 452

6

Beta strand

455 – 458

4

Turn

463 – 465

3

Beta strand

469 – 472

4

Helix

478 – 480

3

Beta strand

482 – 484

3

Beta strand

490 – 492

3

Beta strand

495 – 498

4

Beta strand

509 – 512

4

Helix

518 – 520

3

Beta strand

522 – 525

4

Turn

526 – 529

4

Beta strand

530 – 533

4

Beta strand

536 – 541

6

Helix

545 – 547

3

Beta strand

551 – 554

4

Helix

559 – 561

3

Beta strand

564 – 567

4

Sequences

	Sequence		Length	Mass (Da)
	Q10471 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: D9A0F5D17C55BAF2	FASTA	571	64,733
	10 20 30 40 50 60 MRRRSRMLLC FAFLWVLGIA YYMYSGGGSA LAGGAGGGAG RKEDWNEIDP IKKKDLHHSN 70 80 90 100 110 120 GEEKAQSMET LPPGKVRWPD FNQEAYVGGT MVRSGQDPYA RNKFNQVESD KLRMDRAIPD 130 140 150 160 170 180 TRHDQCQRKQ WRVDLPATSV VITFHNEARS ALLRTVVSVL KKSPPHLIKE IILVDDYSND 190 200 210 220 230 240 PEDGALLGKI EKVRVLRNDR REGLMRSRVR GADAAQAKVL TFLDSHCECN EHWLEPLLER 250 260 270 280 290 300 VAEDRTRVVS PIIDVINMDN FQYVGASADL KGGFDWNLVF KWDYMTPEQR RSRQGNPVAP 310 320 330 340 350 360 IKTPMIAGGL FVMDKFYFEE LGKYDMMMDV WGGENLEISF RVWQCGGSLE IIPCSRVGHV 370 380 390 400 410 420 FRKQHPYTFP GGSGTVFARN TRRAAEVWMD EYKNFYYAAV PSARNVPYGN IQSRLELRKK 430 440 450 460 470 480 LSCKPFKWYL ENVYPELRVP DHQDIAFGAL QQGTNCLDTL GHFADGVVGV YECHNAGGNQ 490 500 510 520 530 540 EWALTKEKSV KHMDLCLTVV DRAPGSLIKL QGCRENDSRQ KWEQIEGNSK LRHVGSNLCL 550 560 570 DSRTAKSGGL SVEVCGPALS QQWKFTLNLQ Q

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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], 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], VARIANT MET-554. Tissue: Hippocampus.
[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]	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. , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases 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]. 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]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]	"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB." Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R. Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract] 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.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 2

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X85019 mRNA. Translation: CAA59381.1.
AK290048 mRNA. Translation: BAF82737.1.
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.

PIR

I37405.

RefSeq

NP_004472.1. NM_004481.3.

UniGene

Hs.743964.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FFU	X-ray	1.64	A	75-571	[»]
2FFV	X-ray	2.75	A/B	75-571	[»]

ProteinModelPortal

Q10471.

SMR

Q10471. Positions 75-568.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

108862. 8 interactions.

MINT

MINT-3026412.

STRING

9606.ENSP00000355632.

Protein family/group databases

CAZy

CBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

PTM databases

PhosphoSite

Q10471.

Polymorphism databases

DMDM

51315838.

Proteomic databases

PaxDb

Q10471.

PeptideAtlas

Q10471.

PRIDE

Q10471.

Protocols and materials databases

DNASU

2590.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000366672; ENSP00000355632; ENSG00000143641.

GeneID

2590.

KEGG

hsa:2590.

UCSC

uc010pwa.1. human.

Organism-specific databases

CTD

2590.

GeneCards

GC01P230193.

H-InvDB

HIX0001682.

HGNC

HGNC:4124. GALNT2.

HPA

HPA011222.

MIM

602274. gene.

neXtProt

NX_Q10471.

PharmGKB

PA28537.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG239675.

HOGENOM

HOG000038227.

HOVERGEN

HBG051699.

InParanoid

Q10471.

KO

K00710.

OMA

DDYSDNP.

OrthoDB

EOG7J9VP2.

TreeFam

TF313267.

Enzyme and pathway databases

BRENDA

2.4.1.41. 2681.

Reactome

REACT_17015. Metabolism of proteins.

UniPathway

UPA00378.

Gene expression databases

ArrayExpress

Q10471.

Bgee

Q10471.

CleanEx

HS_GALNT2.

Genevestigator

Q10471.

Family and domain databases

InterPro

IPR001173. Glyco_trans_2.
IPR000772. Ricin_B_lectin.
[Graphical view]

Pfam

PF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]

SMART

SM00458. RICIN. 1 hit.
[Graphical view]

SUPFAM

SSF50370. SSF50370. 1 hit.

PROSITE

PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

GALNT2. human.

EvolutionaryTrace

Q10471.

GeneWiki

GALNT2.

GenomeRNAi

2590.

NextBio

10245.

PRO

Q10471.

SOURCE

Search...

Entry information

Entry name

GALT2_HUMAN

Accession

Primary (citable) accession number: Q10471
Secondary accession number(s): A8K1Y3, C5HU00, Q9NPY4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	November 1, 1996
Last modified:	February 19, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.