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Q96F25 (ALG14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UDP-N-acetylglucosamine transferase subunit ALG14 homolog
Gene names
Name:ALG14
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length216 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May be involved in protein N-glycosylation. May play a role in the second step of the dolichol-linked oligosaccharide pathway. May anchor the catalytic subunit ALG13 to the ER. Ref.4

Subunit structure

Heterodimer with ALG13 isoform 2to form a functional enzyme By similarity.

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein Probable.

Sequence similarities

Belongs to the ALG14 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 216216UDP-N-acetylglucosamine transferase subunit ALG14 homolog
PRO_0000265116

Regions

Topological domain1 – 33Lumenal Potential
Transmembrane4 – 2421Helical; Potential
Topological domain25 – 216192Cytoplasmic Potential

Natural variations

Natural variant141V → M.
Corresponds to variant rs11165298 [ dbSNP | Ensembl ].
VAR_029635

Sequences

Sequence LengthMass (Da)Tools
Q96F25 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 0724FEAE33A841E8

FASTA21624,151
        10         20         30         40         50         60 
MVCVLVLAAA AGAVAVFLIL RIWVVLRSMD VTPRESLSIL VVAGSGGHTT EILRLLGSLS 

        70         80         90        100        110        120 
NAYSPRHYVI ADTDEMSANK INSFELDRAD RDPSNMYTKY YIHRIPRSRE VQQSWPSTVF 

       130        140        150        160        170        180 
TTLHSMWLSF PLIHRVKPDL VLCNGPGTCV PICVSALLLG ILGIKKVIIV YVESICRVET 

       190        200        210 
LSMSGKILFH LSDYFIVQWP ALKEKYPKSV YLGRIV 

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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].
[2]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. expand/collapse author list , 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].
[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].
Tissue: Pancreas.
[4]"Alg14 recruits Alg13 to the cytoplasmic face of the endoplasmic reticulum to form a novel bipartite UDP-N-acetylglucosamine transferase required for the second step of N-linked glycosylation."
Gao X.-D., Tachikawa H., Sato T., Jigami Y., Dean N.
J. Biol. Chem. 280:36254-36262(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK289395 mRNA. Translation: BAF82084.1.
CH471097 Genomic DNA. Translation: EAW73027.1.
BC011706 mRNA. Translation: AAH11706.1.
RefSeqNP_659425.1. NM_144988.3.
UniGeneHs.408927.

3D structure databases

ProteinModelPortalQ96F25.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid128278. 1 interaction.
STRING9606.ENSP00000359224.

Protein family/group databases

CAZyGT1. Glycosyltransferase Family 1.

PTM databases

PhosphoSiteQ96F25.

Polymorphism databases

DMDM74731649.

Proteomic databases

PaxDbQ96F25.
PRIDEQ96F25.

Protocols and materials databases

DNASU199857.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370205; ENSP00000359224; ENSG00000172339.
GeneID199857.
KEGGhsa:199857.
UCSCuc001dra.2. human.

Organism-specific databases

CTD199857.
GeneCardsGC01M095449.
HGNCHGNC:28287. ALG14.
HPAHPA031829.
MIM612866. gene.
neXtProtNX_Q96F25.
Orphanet353327. Congenital myasthenic syndromes with glycosylation defect.
PharmGKBPA142672628.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0707.
HOGENOMHOG000182099.
HOVERGENHBG059605.
InParanoidQ96F25.
KOK07441.
OMAFTPRFYI.
OrthoDBEOG7SN8DK.
PhylomeDBQ96F25.
TreeFamTF105628.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

BgeeQ96F25.
CleanExHS_ALG14.
GenevestigatorQ96F25.

Family and domain databases

InterProIPR013969. Oligosacch_biosynth_Alg14.
[Graphical view]
PANTHERPTHR12154. PTHR12154. 1 hit.
PfamPF08660. Alg14. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSALG14. human.
GeneWikiALG14.
GenomeRNAi199857.
NextBio89753.
PROQ96F25.
SOURCESearch...

Entry information

Entry nameALG14_HUMAN
AccessionPrimary (citable) accession number: Q96F25
Secondary accession number(s): A8K030
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM