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Protein

Polypeptide N-acetylgalactosaminyltransferase-like 6

Gene

GALNTL6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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.By similarity

Catalytic activityi

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

Cofactori

Mn2+By similarity

Pathway:iprotein glycosylation

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei180 – 1801SubstrateBy similarity
Binding sitei209 – 2091SubstrateBy similarity
Metal bindingi232 – 2321ManganeseBy similarity
Binding sitei233 – 2331SubstrateBy similarity
Metal bindingi234 – 2341ManganeseBy similarity
Binding sitei337 – 3371SubstrateBy similarity
Metal bindingi365 – 3651ManganeseBy similarity
Binding sitei368 – 3681SubstrateBy similarity
Binding sitei373 – 3731SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

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-like 6 (EC:2.4.1.41)
Alternative name(s):
Polypeptide GalNAc transferase 17
Short name:
GalNAc-T17
Short name:
pp-GaNTase 17
Protein-UDP acetylgalactosaminyltransferase 17
Putative polypeptide N-acetylgalactosaminyltransferase 17
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 17
Gene namesi
Name:GALNTL6
Synonyms:GALNT17
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:33844. GALNTL6.

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 – 601573LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164720162.

Polymorphism and mutation databases

BioMutaiGALNTL6.
DMDMi296434516.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 601601Polypeptide N-acetylgalactosaminyltransferase-like 6PRO_0000325774Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi130 ↔ 360PROSITE-ProRule annotation
Glycosylationi141 – 1411N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi351 ↔ 427PROSITE-ProRule annotation
Disulfide bondi466 ↔ 483PROSITE-ProRule annotation
Disulfide bondi518 ↔ 533PROSITE-ProRule annotation
Disulfide bondi558 ↔ 573PROSITE-ProRule annotation
Glycosylationi588 – 5881N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ49A17.
PaxDbiQ49A17.
PRIDEiQ49A17.

Expressioni

Gene expression databases

BgeeiQ49A17.
CleanExiHS_GALNTL6.
ExpressionAtlasiQ49A17. baseline.
GenevisibleiQ49A17. HS.

Organism-specific databases

HPAiHPA031019.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000423313.

Structurei

3D structure databases

ProteinModelPortaliQ49A17.
SMRiQ49A17. Positions 63-598.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini453 – 585133Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni139 – 248110Catalytic subdomain AAdd
BLAST
Regioni306 – 36863Catalytic 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

Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG239675.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ49A17.
KOiK00710.
OMAiNEHWTTL.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ49A17.
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.

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

Isoform 1 (identifier: Q49A17-1) [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
MKRKQKRFLQ MTLLFTVALI FLPNVGLWSL YKDKHLVKSA EPGEQQTFPL
60 70 80 90 100
GLGDGQFYSW TDGLRRKDWH DYESIQKEAM RSGKGEHGKP YPLTEEDHDD
110 120 130 140 150
SAYRENGFNI FVSNNIALER SLPDIRHANC KHKMYLERLP NTSIIIPFHN
160 170 180 190 200
EGWTSLLRTI HSIINRTPGS LIAEIILVDD FSEREHLKDK LEEYMARFSK
210 220 230 240 250
VRIVRTKKRE GLIRTRLLGA SMARGEVLTF LDSHCEVNVN WLPPLLNQIA
260 270 280 290 300
LNHKTIVCPM IDVIDHNHFG YEAQAGDAMR GAFDWEMYYK RIPIPPELQR
310 320 330 340 350
ADPSDPFESP VMAGGLFAVD RKWFWELGGY DPGLEIWGGE QYEISFKVWM
360 370 380 390 400
CGGEMFDVPC SRVGHIYRKY VPYKVPSGTS LARNLKRVAE TWMDEFAEYI
410 420 430 440 450
YQRRPEYRHL STGDISAQKE LRKQLKCKDF KWFMAAVAWD VPKYYPPVEP
460 470 480 490 500
PPAAWGEIRN VAANLCVDSK HGATGTELRL DICVKDGSER TWSHEQLFTF
510 520 530 540 550
GWREDIRPGE PLHTRKFCFD AISHNSPVTL YDCHGMKGNQ LWGYRKDRTL
560 570 580 590 600
FHPVSNSCMD CNPAEKKIFM ARCDPLSETQ QWIFEHINMT VLEKFNHHAN

S
Length:601
Mass (Da):69,788
Last modified:May 18, 2010 - v2
Checksum:iDEFBE2E41DD2FC1D
GO
Isoform 2 (identifier: Q49A17-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-45: MKRKQKRFLQMTLLFTVALIFLPNVGLWSLYKDKHLVKSAEPGEQ → MRAKFRAGAGHQRNPSISADHGVHELVY

Show »
Length:584
Mass (Da):67,589
Checksum:i5A97ED40D9AB1E8F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 831G → R in AAH47551 (PubMed:15489334).Curated
Sequence conflicti250 – 2501A → P in AAH47551 (PubMed:15489334).Curated
Sequence conflicti563 – 5631P → H in AAH47551 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4545MKRKQ…EPGEQ → MRAKFRAGAGHQRNPSISAD HGVHELVY in isoform 2. 1 PublicationVSP_032402Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ626725 mRNA. Translation: CAF25036.1.
AC024706 Genomic DNA. No translation available.
AC025561 Genomic DNA. No translation available.
AC025821 Genomic DNA. No translation available.
AC093803 Genomic DNA. No translation available.
AC095045 Genomic DNA. No translation available.
AC095063 Genomic DNA. No translation available.
AC097496 Genomic DNA. No translation available.
AC105285 Genomic DNA. No translation available.
AC108064 Genomic DNA. No translation available.
AC109520 Genomic DNA. No translation available.
AC110776 Genomic DNA. No translation available.
AC131952 Genomic DNA. No translation available.
BC047551 mRNA. Translation: AAH47551.1.
CCDSiCCDS34104.1. [Q49A17-1]
RefSeqiNP_001030017.2. NM_001034845.2. [Q49A17-1]
UniGeneiHs.386236.

Genome annotation databases

EnsembliENST00000506823; ENSP00000423313; ENSG00000174473.
ENST00000508122; ENSP00000423827; ENSG00000174473. [Q49A17-2]
GeneIDi442117.
KEGGihsa:442117.
UCSCiuc003isv.3. human. [Q49A17-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ626725 mRNA. Translation: CAF25036.1.
AC024706 Genomic DNA. No translation available.
AC025561 Genomic DNA. No translation available.
AC025821 Genomic DNA. No translation available.
AC093803 Genomic DNA. No translation available.
AC095045 Genomic DNA. No translation available.
AC095063 Genomic DNA. No translation available.
AC097496 Genomic DNA. No translation available.
AC105285 Genomic DNA. No translation available.
AC108064 Genomic DNA. No translation available.
AC109520 Genomic DNA. No translation available.
AC110776 Genomic DNA. No translation available.
AC131952 Genomic DNA. No translation available.
BC047551 mRNA. Translation: AAH47551.1.
CCDSiCCDS34104.1. [Q49A17-1]
RefSeqiNP_001030017.2. NM_001034845.2. [Q49A17-1]
UniGeneiHs.386236.

3D structure databases

ProteinModelPortaliQ49A17.
SMRiQ49A17. Positions 63-598.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000423313.

Protein family/group databases

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

Polymorphism and mutation databases

BioMutaiGALNTL6.
DMDMi296434516.

Proteomic databases

MaxQBiQ49A17.
PaxDbiQ49A17.
PRIDEiQ49A17.

Protocols and materials databases

DNASUi442117.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000506823; ENSP00000423313; ENSG00000174473.
ENST00000508122; ENSP00000423827; ENSG00000174473. [Q49A17-2]
GeneIDi442117.
KEGGihsa:442117.
UCSCiuc003isv.3. human. [Q49A17-1]

Organism-specific databases

CTDi442117.
GeneCardsiGC04P172735.
HGNCiHGNC:33844. GALNTL6.
HPAiHPA031019.
MIMi615138. gene.
neXtProtiNX_Q49A17.
PharmGKBiPA164720162.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG239675.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ49A17.
KOiK00710.
OMAiNEHWTTL.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ49A17.
TreeFamiTF313267.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiREACT_115606. O-linked glycosylation of mucins.

Miscellaneous databases

GenomeRNAii442117.
NextBioi110727.
PROiQ49A17.
SOURCEiSearch...

Gene expression databases

BgeeiQ49A17.
CleanExiHS_GALNTL6.
ExpressionAtlasiQ49A17. baseline.
GenevisibleiQ49A17. HS.

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. "The GalNAc-transferase gene family."
    Bennett E.P.
    Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. "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].
  3. "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.

Entry informationi

Entry nameiGLTL6_HUMAN
AccessioniPrimary (citable) accession number: Q49A17
Secondary accession number(s): Q2L4S6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: May 18, 2010
Last modified: July 22, 2015
This is version 87 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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.