Q7Z7M9 (GALT5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Polypeptide N-acetylgalactosaminyltransferase 5
EC=2.4.1.41

Alternative name(s):
Polypeptide GalNAc transferase 5
Short name=GalNAc-T5
Short name=pp-GaNTase 5
Protein-UDP acetylgalactosaminyltransferase 5
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5

Gene names

Name:

GALNT5

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 › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	940 AA.
Sequence status	Complete.
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 activity toward EA2 peptide substrate, but has a weak activity toward Muc2 or Muc1b substrates By similarity.
Catalytic activity	UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.
Cofactor	Manganese By similarity. Calcium By similarity.
Pathway	Protein modification; protein glycosylation.
Subunit structure	Interacts with EXT2. Does not interact with EXT1, EXTL1 or EXTL3. Ref.6
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein By similarity.
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
Coding sequence diversity	Polymorphism
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Calcium Lectin Manganese
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	O-glycan processing Traceable author statement. Source: Reactome glycosaminoglycan biosynthetic process Traceable author statement Ref.6. Source: UniProtKB post-translational protein modification Traceable author statement. Source: Reactome
Cellular_component	Golgi membrane Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	polypeptide N-acetylgalactosaminyltransferase activity Inferred from direct assay Ref.6. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 940	940	Polypeptide N-acetylgalactosaminyltransferase 5		PRO_0000059110
Regions
	Topological domain	1 – 12	12	Cytoplasmic Potential
	Transmembrane	13 – 35	23	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	36 – 940	905	Lumenal Potential
	Domain	804 – 935	132	Ricin B-type lectin
	Region	495 – 604	110	Catalytic subdomain A
	Region	664 – 726	63	Catalytic subdomain B
Amino acid modifications
	Glycosylation	217	1	N-linked (GlcNAc...) Potential
	Glycosylation	256	1	N-linked (GlcNAc...) Potential
	Glycosylation	273	1	N-linked (GlcNAc...) Potential
	Glycosylation	316	1	N-linked (GlcNAc...) Potential
	Glycosylation	362	1	N-linked (GlcNAc...) Potential
	Glycosylation	395	1	N-linked (GlcNAc...) Potential
	Glycosylation	406	1	N-linked (GlcNAc...) Potential
	Glycosylation	578	1	N-linked (GlcNAc...) Potential
	Glycosylation	776	1	N-linked (GlcNAc...) Potential
	Glycosylation	827	1	N-linked (GlcNAc...) Potential
	Glycosylation	845	1	N-linked (GlcNAc...) Potential
	Glycosylation	912	1	N-linked (GlcNAc...) Potential
	Disulfide bond	822 ↔ 835		By similarity
	Disulfide bond	858 ↔ 873		By similarity
	Disulfide bond	908 ↔ 923		By similarity
Natural variations
	Natural variant	77	1	P → L. Corresponds to variant rs3739112 [ dbSNP | Ensembl ].		VAR_019578
	Natural variant	489	1	Q → H. Corresponds to variant rs6759356 [ dbSNP | Ensembl ].		VAR_019579
	Natural variant	507	1	E → D in a breast cancer sample; somatic mutation. Ref.9		VAR_035991
	Natural variant	692	1	L → F in a breast cancer sample; somatic mutation. Ref.9		VAR_035992
Experimental info
	Sequence conflict	273 – 275	3	NTS → AEG Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q7Z7M9 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: DB2DFACDCACD0F6A	FASTA	940	106,266
	10 20 30 40 50 60 MNRIRKFFRG SGRVLAFIFV ASVIWLLFDM AALRLSFSEI NTRVIKEDIV RRERIGFRVQ 70 80 90 100 110 120 PDQGKIFYSS IKEMKPPLRG HGKGAWGKEN VRKTEESVLK VEVDLDQTQR ERKMQNALGR 130 140 150 160 170 180 GKVVPLWHPA HLQTLPVTPN KQKTDGRGTK PEASSHQGTP KQTTAQGAPK TSFIAAKGTQ 190 200 210 220 230 240 VVKISVHMGR VSLKQEPRKS HSPSSDTSKL AAERDLNVTI SLSTDRPKQR SQAVANERAH 250 260 270 280 290 300 PASTAVPKSG EAMALNKTKT QSKEVNANKH KANTSLPFPK FTVNSNRLRK QSINETPLGS 310 320 330 340 350 360 LSKDDGARGA HGKKLNFSES HLVIITKEEE QKADPKEVSN SKTKTIFPKV LGKSQSKHIS 370 380 390 400 410 420 RNRSEMSSSS LAPHRVPLSQ TNHALTGGLE PAKINITAKA PSTEYNQSHI KALLPEDSGT 430 440 450 460 470 480 HQVLRIDVTL SPRDPKAPGQ FGRPVVVPHG KEKEAERRWK EGNFNVYLSD LIPVDRAIED 490 500 510 520 530 540 TRPAGCAEQL VHNNLPTTSV IMCFVDEVWS TLLRSVHSVI NRSPPHLIKE ILLVDDFSTK 550 560 570 580 590 600 DYLKDNLDKY MSQFPKVRIL RLKERHGLIR ARLAGAQNAT GDVLTFLDSH VECNVGWLEP 610 620 630 640 650 660 LLERVYLSRK KVACPVIEVI NDKDMSYMTV DNFQRGIFVW PMNFGWRTIP PDVIAKNRIK 670 680 690 700 710 720 ETDTIRCPVM AGGLFSIDKS YFFELGTYDP GLDVWGGENM ELSFKVWMCG GEIEIIPCSR 730 740 750 760 770 780 VGHIFRNDNP YSFPKDRMKT VERNLVRVAE VWLDEYKELF YGHGDHLIDQ GLDVGNLTQQ 790 800 810 820 830 840 RELRKKLKCK SFKWYLENVF PDLRAPIVRA SGVLINVALG KCISIENTTV ILEDCDGSKE 850 860 870 880 890 900 LQQFNYTWLR LIKCGEWCIA PIPDKGAVRL HPCDNRNKGL KWLHKSTSVF HPELVNHIVF 910 920 930 940 ENNQQLLCLE GNFSQKILKV AACDPVKPYQ KWKFEKYYEA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Huang C.Q., Wu S.L., Cheng Z. Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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]. Tissue: Synovium.
[3]	Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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].
[5]	Bennett E.P. Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 273-940.
[6]	"A direct interaction between EXT proteins and glycosyltransferases is defective in hereditary multiple exostoses." Simmons A.D., Musy M.M., Lopes C.S., Hwang L.-Y., Yang Y.-P., Lovett M. Hum. Mol. Genet. 8:2155-2164(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 331-940, INTERACTION WITH EXT2.
[7]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[8]	"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].
[9]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASP-507 AND PHE-692.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 5

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY277591 mRNA. Translation: AAP34404.1. AK292154 mRNA. Translation: BAF84843.1. CH471058 Genomic DNA. Translation: EAX11449.1. BC142676 mRNA. Translation: AAI42677.1. AJ245539 mRNA. Translation: CAB65104.1. AF154107 mRNA. Translation: AAF15313.1.
IPI	IPI00005401.
RefSeq	NP_055383.1. NM_014568.1.
UniGene	Hs.269027.
3D structure databases
ProteinModelPortal	Q7Z7M9.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000259056.
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
PTM databases
PhosphoSite	Q7Z7M9.
Polymorphism databases
DMDM	51315940.
Proteomic databases
PaxDb	Q7Z7M9.
PRIDE	Q7Z7M9.
Protocols and materials databases
DNASU	11227.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000259056; ENSP00000259056; ENSG00000136542.
GeneID	11227.
KEGG	hsa:11227.
UCSC	uc002tzg.3. human.
Organism-specific databases
CTD	11227.
GeneCards	GC02P158079.
HGNC	HGNC:4127. GALNT5.
HPA	HPA008963. HPA009035.
neXtProt	NX_Q7Z7M9.
PharmGKB	PA28540.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG307550.
HOGENOM	HOG000231869.
HOVERGEN	HBG051698.
InParanoid	Q7Z7M9.
KO	K00710.
OMA	EGNFSQK.
OrthoDB	EOG41G33C.
PhylomeDB	Q7Z7M9.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	Q7Z7M9.
Bgee	Q7Z7M9.
CleanEx	HS_GALNT5.
Genevestigator	Q7Z7M9.
GermOnline	ENSG00000136542. Homo sapiens.
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. RicinB_like. 1 hit.
PROSITE	PS50231. RICIN_B_LECTIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	GALNT5. human.
GenomeRNAi	11227.
NextBio	42730.

Entry information

Entry name

GALT5_HUMAN

Accession

Primary (citable) accession number: Q7Z7M9
Secondary accession number(s): A5PKZ1, Q9UGK7, Q9UHL6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	October 1, 2003
Last modified:	May 1, 2013
This is version 85 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.