Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8NCW6

- GLT11_HUMAN

UniProt

Q8NCW6 - GLT11_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Polypeptide N-acetylgalactosaminyltransferase 11

Gene

GALNT11

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

Functioni

Polypeptide N-acetylgalactosaminyltransferase that catalyzes the initiation of protein O-linked glycosylation and is involved in left/right asymmetry by mediating O-glycosylation of NOTCH1. O-glycosylation of NOTCH1 promotes activation of NOTCH1, modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO). Polypeptide N-acetylgalactosaminyltransferases catalyze the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Displays the same enzyme activity toward MUC1, MUC4, and EA2 than GALNT1. Not involved in glycosylation of erythropoietin (EPO).2 Publications

Catalytic activityi

UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.1 Publication

Cofactori

Manganese.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei191 – 1911SubstrateBy similarity
Binding sitei222 – 2221SubstrateBy similarity
Metal bindingi245 – 2451ManganeseBy similarity
Binding sitei246 – 2461SubstrateBy similarity
Metal bindingi247 – 2471ManganeseBy similarity
Binding sitei350 – 3501SubstrateBy similarity
Metal bindingi378 – 3781ManganeseBy similarity
Binding sitei381 – 3811SubstrateBy similarity
Binding sitei386 – 3861SubstrateBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. cilium morphogenesis Source: UniProtKB
  3. determination of left/right symmetry Source: UniProtKB
  4. Notch receptor processing Source: UniProtKB
  5. Notch signaling involved in heart development Source: UniProtKB
  6. O-glycan processing Source: Reactome
  7. post-translational protein modification Source: Reactome
  8. protein O-linked glycosylation via threonine Source: UniProtKB
  9. regulation of Notch signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Notch signaling pathway

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi2.4.1.41. 2681.
ReactomeiREACT_115606. O-linked glycosylation of mucins.
SABIO-RKQ8NCW6.
UniPathwayiUPA00378.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Polypeptide N-acetylgalactosaminyltransferase 11 (EC:2.4.1.41)
Alternative name(s):
Polypeptide GalNAc transferase 11
Short name:
GalNAc-T11
Short name:
pp-GaNTase 11
Protein-UDP acetylgalactosaminyltransferase 11
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11
Gene namesi
Name:GALNT11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:19875. GALNT11.

Subcellular locationi

Golgi apparatus membrane 1 Publication; Single-pass type II membrane protein 1 Publication

GO - Cellular componenti

  1. Golgi membrane Source: Reactome
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Defects in GALNT11 may be a cause of heterotaxy, a congenital heart disease resulting from abnormalities in left-right (LR) body patterning.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi247 – 2471H → A: Abolishes glycosyltransferase activity and ability to rescue left-right patterning defects induced by galnt11 knockdown in X.tropicalis. 1 Publication

Keywords - Diseasei

Heterotaxy

Organism-specific databases

PharmGKBiPA134911149.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 608608Polypeptide N-acetylgalactosaminyltransferase 11PRO_0000059125Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi141 ↔ 373PROSITE-ProRule annotation
Disulfide bondi364 ↔ 441PROSITE-ProRule annotation
Glycosylationi428 – 4281N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi493 ↔ 512PROSITE-ProRule annotation
Disulfide bondi536 ↔ 553PROSITE-ProRule annotation
Disulfide bondi578 ↔ 596PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ8NCW6.
PaxDbiQ8NCW6.
PRIDEiQ8NCW6.

PTM databases

PhosphoSiteiQ8NCW6.

Expressioni

Tissue specificityi

Highly expressed in kidney. Expressed at intermediate level in brain, heart and skeletal muscle. Weakly expressed other tissues. In kidney, it is strongly expressed in tubules but not expressed in glomeruli.1 Publication

Gene expression databases

BgeeiQ8NCW6.
CleanExiHS_GALNT11.
ExpressionAtlasiQ8NCW6. baseline and differential.
GenevestigatoriQ8NCW6.

Organism-specific databases

HPAiHPA039330.

Interactioni

Subunit structurei

Interacts with NOTCH1.1 Publication

Protein-protein interaction databases

BioGridi121988. 10 interactions.
STRINGi9606.ENSP00000315835.

Structurei

3D structure databases

ProteinModelPortaliQ8NCW6.
SMRiQ8NCW6. Positions 114-606.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence Analysis
Topological domaini30 – 608579LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei7 – 2923Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini476 – 607132Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni150 – 261112Catalytic subdomain AAdd
BLAST
Regioni319 – 38163Catalytic 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.
InParanoidiQ8NCW6.
KOiK00710.
OMAiMIFNERD.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ8NCW6.
TreeFamiTF313267.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR027791. Galactosyl_T_C.
IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF02709. Glyco_transf_7C. 1 hit.
PF00535. 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. Align

Isoform 1 (identifier: Q8NCW6) [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
MGSVTVRYFC YGCLFTSATW TVLLFVYFNF SEVTQPLKNV PVKGSGPHGP
60 70 80 90 100
SPKKFYPRFT RGPSRVLEPQ FKANKIDDVI DSRVEDPEEG HLKFSSELGM
110 120 130 140 150
IFNERDQELR DLGYQKHAFN MLISDRLGYH RDVPDTRNAA CKEKFYPPDL
160 170 180 190 200
PAASVVICFY NEAFSALLRT VHSVIDRTPA HLLHEIILVD DDSDFDDLKG
210 220 230 240 250
ELDEYVQKYL PGKIKVIRNT KREGLIRGRM IGAAHATGEV LVFLDSHCEV
260 270 280 290 300
NVMWLQPLLA AIREDRHTVV CPVIDIISAD TLAYSSSPVV RGGFNWGLHF
310 320 330 340 350
KWDLVPLSEL GRAEGATAPI KSPTMAGGLF AMNRQYFHEL GQYDSGMDIW
360 370 380 390 400
GGENLEISFR IWMCGGKLFI IPCSRVGHIF RKRRPYGSPE GQDTMTHNSL
410 420 430 440 450
RLAHVWLDEY KEQYFSLRPD LKTKSYGNIS ERVELRKKLG CKSFKWYLDN
460 470 480 490 500
VYPEMQISGS HAKPQQPIFV NRGPKRPKVL QRGRLYHLQT NKCLVAQGRP
510 520 530 540 550
SQKGGLVVLK ACDYSDPNQI WIYNEEHELV LNSLLCLDMS ETRSSDPPRL
560 570 580 590 600
MKCHGSGGSQ QWTFGKNNRL YQVSVGQCLR AVDPLGQKGS VAMAICDGSS

SQQWHLEG
Length:608
Mass (Da):68,919
Last modified:August 16, 2004 - v2
Checksum:i075D7B839A8D5607
GO
Isoform 2 (identifier: Q8NCW6-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     196-202: DDLKGEL → GKECCTW
     203-608: Missing.

Note: No experimental confirmation available.

Show »
Length:202
Mass (Da):23,090
Checksum:iA2B98F18AB31C370
GO

Sequence cautioni

The sequence BAB15338.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941F → L in BAG54116. (PubMed:14702039)Curated
Sequence conflicti551 – 5511M → V in BAB15105. (PubMed:14702039)Curated
Sequence conflicti577 – 5771Q → L in BAB15105. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti151 – 1511P → S.
Corresponds to variant rs6464201 [ dbSNP | Ensembl ].
VAR_019589
Natural varianti197 – 1971D → Y.1 Publication
Corresponds to variant rs3778922 [ dbSNP | Ensembl ].
VAR_019590

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei196 – 2027DDLKGEL → GKECCTW in isoform 2. 1 PublicationVSP_011215
Alternative sequencei203 – 608406Missing in isoform 2. 1 PublicationVSP_011216Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y12434 mRNA. Translation: CAC79625.3.
AK025287 mRNA. Translation: BAB15105.1.
AK026056 mRNA. Translation: BAB15338.1. Different initiation.
AK124934 mRNA. Translation: BAG54116.1.
AC006017 Genomic DNA. Translation: AAD45821.1.
BC059377 mRNA. Translation: AAH59377.1.
CCDSiCCDS5930.1. [Q8NCW6-1]
RefSeqiNP_071370.2. NM_022087.2. [Q8NCW6-1]
XP_006716145.1. XM_006716082.1. [Q8NCW6-1]
XP_006716146.1. XM_006716083.1. [Q8NCW6-1]
XP_006716147.1. XM_006716084.1. [Q8NCW6-1]
UniGeneiHs.647109.

Genome annotation databases

EnsembliENST00000415421; ENSP00000410093; ENSG00000178234. [Q8NCW6-2]
ENST00000422997; ENSP00000389449; ENSG00000178234. [Q8NCW6-2]
ENST00000430044; ENSP00000395122; ENSG00000178234. [Q8NCW6-1]
ENST00000434507; ENSP00000416787; ENSG00000178234. [Q8NCW6-1]
GeneIDi63917.
KEGGihsa:63917.
UCSCiuc003wku.2. human. [Q8NCW6-1]
uc003wkv.1. human. [Q8NCW6-2]

Polymorphism databases

DMDMi51316030.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 11

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y12434 mRNA. Translation: CAC79625.3 .
AK025287 mRNA. Translation: BAB15105.1 .
AK026056 mRNA. Translation: BAB15338.1 . Different initiation.
AK124934 mRNA. Translation: BAG54116.1 .
AC006017 Genomic DNA. Translation: AAD45821.1 .
BC059377 mRNA. Translation: AAH59377.1 .
CCDSi CCDS5930.1. [Q8NCW6-1 ]
RefSeqi NP_071370.2. NM_022087.2. [Q8NCW6-1 ]
XP_006716145.1. XM_006716082.1. [Q8NCW6-1 ]
XP_006716146.1. XM_006716083.1. [Q8NCW6-1 ]
XP_006716147.1. XM_006716084.1. [Q8NCW6-1 ]
UniGenei Hs.647109.

3D structure databases

ProteinModelPortali Q8NCW6.
SMRi Q8NCW6. Positions 114-606.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121988. 10 interactions.
STRINGi 9606.ENSP00000315835.

Protein family/group databases

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

PTM databases

PhosphoSitei Q8NCW6.

Polymorphism databases

DMDMi 51316030.

Proteomic databases

MaxQBi Q8NCW6.
PaxDbi Q8NCW6.
PRIDEi Q8NCW6.

Protocols and materials databases

DNASUi 63917.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000415421 ; ENSP00000410093 ; ENSG00000178234 . [Q8NCW6-2 ]
ENST00000422997 ; ENSP00000389449 ; ENSG00000178234 . [Q8NCW6-2 ]
ENST00000430044 ; ENSP00000395122 ; ENSG00000178234 . [Q8NCW6-1 ]
ENST00000434507 ; ENSP00000416787 ; ENSG00000178234 . [Q8NCW6-1 ]
GeneIDi 63917.
KEGGi hsa:63917.
UCSCi uc003wku.2. human. [Q8NCW6-1 ]
uc003wkv.1. human. [Q8NCW6-2 ]

Organism-specific databases

CTDi 63917.
GeneCardsi GC07P151722.
H-InvDB HIX0007236.
HGNCi HGNC:19875. GALNT11.
HPAi HPA039330.
MIMi 615130. gene.
neXtProti NX_Q8NCW6.
PharmGKBi PA134911149.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG239675.
GeneTreei ENSGT00760000118828.
HOGENOMi HOG000038227.
HOVERGENi HBG051699.
InParanoidi Q8NCW6.
KOi K00710.
OMAi MIFNERD.
OrthoDBi EOG7J9VP2.
PhylomeDBi Q8NCW6.
TreeFami TF313267.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BRENDAi 2.4.1.41. 2681.
Reactomei REACT_115606. O-linked glycosylation of mucins.
SABIO-RK Q8NCW6.

Miscellaneous databases

ChiTaRSi GALNT11. human.
GenomeRNAii 63917.
NextBioi 65642.
PROi Q8NCW6.
SOURCEi Search...

Gene expression databases

Bgeei Q8NCW6.
CleanExi HS_GALNT11.
ExpressionAtlasi Q8NCW6. baseline and differential.
Genevestigatori Q8NCW6.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR027791. Galactosyl_T_C.
IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view ]
Pfami PF02709. Glyco_transf_7C. 1 hit.
PF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view ]
SMARTi SM00458. RICIN. 1 hit.
[Graphical view ]
SUPFAMi SSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEi PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Functional conservation of subfamilies of putative UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases in Drosophila, Caenorhabditis elegans, and mammals. One subfamily composed of l(2)35Aa is essential in Drosophila."
    Schwientek T., Bennett E.P., Flores C., Thacker J., Hollmann M., Reis C.A., Behrens J., Mandel U., Keck B., Schaefer M.A., Haselmann K., Zubarev R., Roepstorff P., Burchell J.M., Taylor-Papadimitriou J., Hollingsworth M.A., Clausen H.
    J. Biol. Chem. 277:22623-22638(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. Bennett E.P.
    Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 14-15; 119; 295; 310; 365 AND 369.
  3. "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] (ISOFORM 1).
    Tissue: Colon, Kidney epithelium and Subthalamic nucleus.
  4. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 2).
    Tissue: Placenta.
  6. "Rare copy number variations in congenital heart disease patients identify unique genes in left-right patterning."
    Fakhro K.A., Choi M., Ware S.M., Belmont J.W., Towbin J.A., Lifton R.P., Khokha M.K., Brueckner M.
    Proc. Natl. Acad. Sci. U.S.A. 108:2915-2920(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE INVOLVEMENT IN HETEROTAXY.
  7. "The heterotaxy gene GALNT11 glycosylates Notch to orchestrate cilia type and laterality."
    Boskovski M.T., Yuan S., Pedersen N.B., Goth C.K., Makova S., Clausen H., Brueckner M., Khokha M.K.
    Nature 504:456-459(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF HIS-247, INTERACTION WITH NOTCH1.
  8. Cited for: VARIANT TYR-197.

Entry informationi

Entry nameiGLT11_HUMAN
AccessioniPrimary (citable) accession number: Q8NCW6
Secondary accession number(s): B3KWF4
, Q6PCD1, Q9H6C2, Q9H6Z5, Q9UDR8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: October 29, 2014
This is version 110 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 7
    Human chromosome 7: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3