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Protein

Polypeptide N-acetylgalactosaminyltransferase

Gene

Galnt2

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Cofactori

Mn2+UniRule annotation

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.UniRule annotationSAAS annotation
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

GlycosyltransferaseUniRule annotationSAAS annotation, Transferase

Keywords - Ligandi

LectinUniRule annotationSAAS annotation, ManganeseUniRule annotationSAAS annotation

Enzyme and pathway databases

ReactomeiR-RNO-6811436. COPI-independent Golgi-to-ER retrograde traffic.
R-RNO-913709. O-linked glycosylation of mucins.
UniPathwayiUPA00378.

Names & Taxonomyi

Protein namesi
Recommended name:
Polypeptide N-acetylgalactosaminyltransferaseUniRule annotation (EC:2.4.1.-UniRule annotation)
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferaseUniRule annotation
Gene namesi
Name:Galnt2Imported
Synonyms:Galnt2_predictedImported
ORF Names:rCG_50888Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 19

Organism-specific databases

RGDi1310692. Galnt2.

Subcellular locationi

  • Golgi apparatus membrane UniRule annotation; Single-pass type II membrane protein UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatusUniRule annotationSAAS annotation, Membrane

PTM / Processingi

Keywords - PTMi

Disulfide bondUniRule annotationSAAS annotation

PTM databases

iPTMnetiD3ZFD2.

Expressioni

Gene expression databases

ExpressionAtlasiD3ZFD2. baseline and differential.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000062956.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini358 – 468111Ricin B-type lectinInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyltransferase 2 family.SAAS annotation
Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.UniRule annotationSAAS annotation
Contains 1 ricin B-type lectin domain.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helixSAAS annotation

Phylogenomic databases

eggNOGiKOG3738. Eukaryota.
ENOG410XPRX. LUCA.
GeneTreeiENSGT00760000118828.
KOiK00710.
OMAiGKVRWPD.
OrthoDBiEOG7J9VP2.
PhylomeDBiD3ZFD2.

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]

Sequencei

Sequence statusi: Complete.

D3ZFD2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METLPPGKVR WPDFNQEAYV GGTMVRSGQD PYARNKFNQV ESDKLRMDRS
60 70 80 90 100
IPDTRHDQCQ RKQWRVDLPA TSVVITFHNE ARSALLRTVV SVLKRSPPHL
110 120 130 140 150
IKEIILVDDY SNDPEDGALL GKIEKVRVLR NDRREGLMRS RVRGADAAQA
160 170 180 190 200
KVLTFLDSHC ECNERWLEPL LERVAEDRTR VVSPIIDVIN MDNFQYVGAS
210 220 230 240 250
ADLKGGFDWN LVFKWDYMTP EQRRSRQGNP VAPIKTPMIA GGLFVMDKLY
260 270 280 290 300
FEELGKYDMM MDVWGGENLE ISFRVWQCGG SLEIIPCSRV GHVFRKQHPY
310 320 330 340 350
TFPGGSGTVF ARIQSRLELR KKLGCKPFKW YLDNVYPELR VPDHQDIAFG
360 370 380 390 400
ALQQGTNCLD TLGHFADGVV GIYECHNAGG NQEWALTKEK SVKHMDLCLT
410 420 430 440 450
VVDRSPGSLI RLQGCRENDS RQKWEQIEGN SKLRHVGSNL CLDSRTAKSG
460 470
GLSVEVCGPA LSQQWKFSLN LQQ
Length:473
Mass (Da):53,783
Last modified:April 20, 2010 - v1
Checksum:iEB77F62C79A8582B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07044086 Genomic DNA. No translation available.
CH474054 Genomic DNA. Translation: EDL96727.1.
RefSeqiNP_001099666.1. NM_001106196.1.
UniGeneiRn.144772.

Genome annotation databases

EnsembliENSRNOT00000065431; ENSRNOP00000062956; ENSRNOG00000019143.
GeneIDi292090.
KEGGirno:292090.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07044086 Genomic DNA. No translation available.
CH474054 Genomic DNA. Translation: EDL96727.1.
RefSeqiNP_001099666.1. NM_001106196.1.
UniGeneiRn.144772.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000062956.

PTM databases

iPTMnetiD3ZFD2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000065431; ENSRNOP00000062956; ENSRNOG00000019143.
GeneIDi292090.
KEGGirno:292090.

Organism-specific databases

CTDi2590.
RGDi1310692. Galnt2.

Phylogenomic databases

eggNOGiKOG3738. Eukaryota.
ENOG410XPRX. LUCA.
GeneTreeiENSGT00760000118828.
KOiK00710.
OMAiGKVRWPD.
OrthoDBiEOG7J9VP2.
PhylomeDBiD3ZFD2.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiR-RNO-6811436. COPI-independent Golgi-to-ER retrograde traffic.
R-RNO-913709. O-linked glycosylation of mucins.

Gene expression databases

ExpressionAtlasiD3ZFD2. baseline and differential.

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. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  2. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  4. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiD3ZFD2_RAT
AccessioniPrimary (citable) accession number: D3ZFD2
Entry historyi
Integrated into UniProtKB/TrEMBL: April 20, 2010
Last sequence update: April 20, 2010
Last modified: June 8, 2016
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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 one 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.