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Q9Y5Z9

- UBIA1_HUMAN

UniProt

Q9Y5Z9 - UBIA1_HUMAN

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Protein
UbiA prenyltransferase domain-containing protein 1
Gene
UBIAD1, TERE1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Prenyltransferase that mediates the formation of menaquinone-4 (MK-4) and coenzyme Q10. MK-4 is a vitamin K2 isoform present at high concentrations in the brain, kidney and pancreas, and is required for endothelial cell development. Mediates the conversion of phylloquinone (PK) into MK-4, probably by cleaving the side chain of phylloquinone (PK) to release 2-methyl-1,4-naphthoquinone (menadione; K3) and then prenylating it with geranylgeranyl pyrophosphate (GGPP) to form MK-4. Also plays a role in cardiovascular development independently of MK-4 biosynthesis, by acting as a coenzyme Q10 biosyntetic enzyme: coenzyme Q10, also named ubiquinone, plays a important antioxidant role in the cardiovascular system. Mediates biosynthesis of coenzyme Q10 in the Golgi membrane, leading to protect cardiovascular tissues from NOS3/eNOS-dependent oxidative stress.2 Publications

Pathwayi

GO - Molecular functioni

  1. antioxidant activity Source: UniProtKB
  2. prenyltransferase activity Source: UniProtKB
  3. protein binding Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. menaquinone biosynthetic process Source: UniProtKB
  2. ubiquinone biosynthetic process Source: UniProtKB
  3. vitamin K biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Prenyltransferase, Transferase

Keywords - Biological processi

Menaquinone biosynthesis, Ubiquinone biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00079.
UPA00232.

Names & Taxonomyi

Protein namesi
Recommended name:
UbiA prenyltransferase domain-containing protein 1 (EC:2.5.1.-)
Alternative name(s):
Transitional epithelial response protein 1
Gene namesi
Name:UBIAD1
Synonyms:TERE1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:30791. UBIAD1.

Subcellular locationi

Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Mitochondrion membrane. Cytoplasm. Nucleus 5 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei83 – 10321Helical; Reviewed prediction
Add
BLAST
Transmembranei134 – 15421Helical; Reviewed prediction
Add
BLAST
Transmembranei160 – 18021Helical; Reviewed prediction
Add
BLAST
Transmembranei188 – 20821Helical; Reviewed prediction
Add
BLAST
Transmembranei209 – 22921Helical; Reviewed prediction
Add
BLAST
Transmembranei245 – 26723Helical; Reviewed prediction
Add
BLAST
Transmembranei277 – 29721Helical; Reviewed prediction
Add
BLAST
Transmembranei315 – 33521Helical; Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. endoplasmic reticulum Source: UniProtKB
  3. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  4. integral component of Golgi membrane Source: UniProtKB
  5. membrane Source: UniProtKB
  6. mitochondrial membrane Source: UniProtKB-SubCell
  7. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Membrane, Mitochondrion, Nucleus

Pathology & Biotechi

Involvement in diseasei

Corneal dystrophy, Schnyder type (SCCD) [MIM:121800]: A form of stromal corneal dystrophy characterized by corneal clouding, resulting from abnormal deposition of cholesterol and phospholipids, and decreased visual acuity. Typically, ring-shaped yellow-white opacities composed of innumerable fine needle-shaped crystals form in Bowman layer and the adjacent anterior stroma of the central cornea. The crystals usually remain in the anterior third of the cornea. The corneal epithelium and endothelium as well as Descemet membrane are spared.
Note: The disease is caused by mutations affecting the gene represented in this entry.9 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti97 – 971A → T in SCCD. 1 Publication
VAR_064337
Natural varianti98 – 981G → S in SCCD. 1 Publication
VAR_064338
Natural varianti102 – 1021N → S in SCCD; reduced menaquinone-4 (MK-4) synthesis; does not affect coenzyme Q10 synthesis. 6 Publications
VAR_043714
Natural varianti112 – 1121D → G in SCCD; does not affect coenzyme Q10 synthesis. 2 Publications
VAR_043715
Natural varianti112 – 1121D → N in SCCD; reduced menaquinone-4 (MK-4) synthesis. 2 Publications
VAR_064339
Natural varianti118 – 1181D → G in SCCD. 1 Publication
VAR_043716
Natural varianti119 – 1191R → G in SCCD. 1 Publication
VAR_043717
Natural varianti121 – 1211L → F in SCCD. 1 Publication
VAR_043718
Natural varianti122 – 1221V → E in SCCD. 1 Publication
VAR_064340
Natural varianti122 – 1221V → G in SCCD. 1 Publication
VAR_064341
Natural varianti171 – 1711S → P in SCCD. 2 Publications
VAR_043719
Natural varianti175 – 1751T → I in SCCD. 2 Publications
VAR_043720
Natural varianti177 – 1771G → E in SCCD; reduced menaquinone-4 (MK-4) synthesis. 1 Publication
VAR_069267
Natural varianti177 – 1771G → R in SCCD; reduced menaquinone-4 (MK-4) synthesis. 3 Publications
VAR_043721
Natural varianti186 – 1861G → R in SCCD. 1 Publication
VAR_043722
Natural varianti188 – 1881L → H in SCCD. 1 Publication
VAR_064342
Natural varianti232 – 2321N → S in SCCD. 1 Publication
VAR_043723
Natural varianti236 – 2361D → E in SCCD. 1 Publication
VAR_043724
Natural varianti240 – 2401D → N in SCCD. 1 Publication
VAR_064343

Keywords - Diseasei

Corneal dystrophy, Disease mutation

Organism-specific databases

MIMi121800. phenotype.
Orphaneti98967. Schnyder corneal dystrophy.
PharmGKBiPA142670660.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 338337UbiA prenyltransferase domain-containing protein 1
PRO_0000242627Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9Y5Z9.
PaxDbiQ9Y5Z9.
PRIDEiQ9Y5Z9.

PTM databases

PhosphoSiteiQ9Y5Z9.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiQ9Y5Z9.
CleanExiHS_UBIAD1.
GenevestigatoriQ9Y5Z9.

Organism-specific databases

HPAiHPA038200.
HPA044862.

Interactioni

Subunit structurei

Interacts with HMGCR and SOAT1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
HMGCRP040355EBI-6621921,EBI-465513
SOAT1P356102EBI-2819725,EBI-6621955
SOAT1P35610-13EBI-2819725,EBI-6621997

Protein-protein interaction databases

BioGridi118958. 1 interaction.
IntActiQ9Y5Z9. 4 interactions.
MINTiMINT-3087699.
STRINGi9606.ENSP00000366006.

Structurei

3D structure databases

ProteinModelPortaliQ9Y5Z9.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1575.
HOGENOMiHOG000231452.
HOVERGENiHBG080284.
InParanoidiQ9Y5Z9.
OMAiRDIEQDK.
OrthoDBiEOG7XH6Q2.
PhylomeDBiQ9Y5Z9.
TreeFamiTF323238.

Family and domain databases

InterProiIPR000537. UbiA_prenyltransferase.
IPR026046. UBIAD1.
[Graphical view]
PfamiPF01040. UbiA. 1 hit.
[Graphical view]
PIRSFiPIRSF005355. UBIAD1. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y5Z9-1) [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

MAASQVLGEK INILSGETVK AGDRDPLGND CPEQDRLPQR SWRQKCASYV    50
LALRPWSFSA SLTPVALGSA LAYRSHGVLD PRLLVGCAVA VLAVHGAGNL 100
VNTYYDFSKG IDHKKSDDRT LVDRILEPQD VVRFGVFLYT LGCVCAACLY 150
YLSPLKLEHL ALIYFGGLSG SFLYTGGIGF KYVALGDLII LITFGPLAVM 200
FAYAIQVGSL AIFPLVYAIP LALSTEAILH SNNTRDMESD REAGIVTLAI 250
LIGPTFSYIL YNTLLFLPYL VFSILATHCT ISLALPLLTI PMAFSLERQF 300
RSQAFNKLPQ RTAKLNLLLG LFYVFGIILA PAGSLPKI 338
Length:338
Mass (Da):36,831
Last modified:November 1, 1999 - v1
Checksum:i02808542DB9EA249
GO
Isoform 2 (identifier: Q9Y5Z9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     177-179: GIG → VLI
     180-338: Missing.

Note: No experimental confirmation available.

Show »
Length:179
Mass (Da):19,482
Checksum:i78C76B7F91C92017
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti75 – 751S → F.1 Publication
Corresponds to variant rs114000606 [ dbSNP | Ensembl ].
VAR_043713
Natural varianti97 – 971A → T in SCCD. 1 Publication
VAR_064337
Natural varianti98 – 981G → S in SCCD. 1 Publication
VAR_064338
Natural varianti102 – 1021N → S in SCCD; reduced menaquinone-4 (MK-4) synthesis; does not affect coenzyme Q10 synthesis. 6 Publications
VAR_043714
Natural varianti112 – 1121D → G in SCCD; does not affect coenzyme Q10 synthesis. 2 Publications
VAR_043715
Natural varianti112 – 1121D → N in SCCD; reduced menaquinone-4 (MK-4) synthesis. 2 Publications
VAR_064339
Natural varianti118 – 1181D → G in SCCD. 1 Publication
VAR_043716
Natural varianti119 – 1191R → G in SCCD. 1 Publication
VAR_043717
Natural varianti121 – 1211L → F in SCCD. 1 Publication
VAR_043718
Natural varianti122 – 1221V → E in SCCD. 1 Publication
VAR_064340
Natural varianti122 – 1221V → G in SCCD. 1 Publication
VAR_064341
Natural varianti171 – 1711S → P in SCCD. 2 Publications
VAR_043719
Natural varianti175 – 1751T → I in SCCD. 2 Publications
VAR_043720
Natural varianti177 – 1771G → E in SCCD; reduced menaquinone-4 (MK-4) synthesis. 1 Publication
VAR_069267
Natural varianti177 – 1771G → R in SCCD; reduced menaquinone-4 (MK-4) synthesis. 3 Publications
VAR_043721
Natural varianti186 – 1861G → R in SCCD. 1 Publication
VAR_043722
Natural varianti188 – 1881L → H in SCCD. 1 Publication
VAR_064342
Natural varianti232 – 2321N → S in SCCD. 1 Publication
VAR_043723
Natural varianti236 – 2361D → E in SCCD. 1 Publication
VAR_043724
Natural varianti240 – 2401D → N in SCCD. 1 Publication
VAR_064343

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei177 – 1793GIG → VLI in isoform 2.
VSP_019455
Alternative sequencei180 – 338159Missing in isoform 2.
VSP_019456Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti163 – 1631I → V in BAD96528. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF117064 mRNA. Translation: AAD27581.1.
BT006832 mRNA. Translation: AAP35478.1.
AK222808 mRNA. Translation: BAD96528.1.
AK074890 mRNA. Translation: BAG52025.1.
AL031291 Genomic DNA. Translation: CAI22837.1.
AL031291 Genomic DNA. Translation: CAI22838.1.
CH471130 Genomic DNA. Translation: EAW71686.1.
BC004468 mRNA. Translation: AAH04468.1.
CCDSiCCDS129.1. [Q9Y5Z9-1]
RefSeqiNP_037451.1. NM_013319.2. [Q9Y5Z9-1]
UniGeneiHs.522933.

Genome annotation databases

EnsembliENST00000376804; ENSP00000366000; ENSG00000120942. [Q9Y5Z9-2]
ENST00000376810; ENSP00000366006; ENSG00000120942. [Q9Y5Z9-1]
GeneIDi29914.
KEGGihsa:29914.
UCSCiuc001asg.3. human. [Q9Y5Z9-1]

Polymorphism databases

DMDMi74753514.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF117064 mRNA. Translation: AAD27581.1 .
BT006832 mRNA. Translation: AAP35478.1 .
AK222808 mRNA. Translation: BAD96528.1 .
AK074890 mRNA. Translation: BAG52025.1 .
AL031291 Genomic DNA. Translation: CAI22837.1 .
AL031291 Genomic DNA. Translation: CAI22838.1 .
CH471130 Genomic DNA. Translation: EAW71686.1 .
BC004468 mRNA. Translation: AAH04468.1 .
CCDSi CCDS129.1. [Q9Y5Z9-1 ]
RefSeqi NP_037451.1. NM_013319.2. [Q9Y5Z9-1 ]
UniGenei Hs.522933.

3D structure databases

ProteinModelPortali Q9Y5Z9.
ModBasei Search...

Protein-protein interaction databases

BioGridi 118958. 1 interaction.
IntActi Q9Y5Z9. 4 interactions.
MINTi MINT-3087699.
STRINGi 9606.ENSP00000366006.

PTM databases

PhosphoSitei Q9Y5Z9.

Polymorphism databases

DMDMi 74753514.

Proteomic databases

MaxQBi Q9Y5Z9.
PaxDbi Q9Y5Z9.
PRIDEi Q9Y5Z9.

Protocols and materials databases

DNASUi 29914.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000376804 ; ENSP00000366000 ; ENSG00000120942 . [Q9Y5Z9-2 ]
ENST00000376810 ; ENSP00000366006 ; ENSG00000120942 . [Q9Y5Z9-1 ]
GeneIDi 29914.
KEGGi hsa:29914.
UCSCi uc001asg.3. human. [Q9Y5Z9-1 ]

Organism-specific databases

CTDi 29914.
GeneCardsi GC01P011334.
HGNCi HGNC:30791. UBIAD1.
HPAi HPA038200.
HPA044862.
MIMi 121800. phenotype.
611632. gene.
neXtProti NX_Q9Y5Z9.
Orphaneti 98967. Schnyder corneal dystrophy.
PharmGKBi PA142670660.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1575.
HOGENOMi HOG000231452.
HOVERGENi HBG080284.
InParanoidi Q9Y5Z9.
OMAi RDIEQDK.
OrthoDBi EOG7XH6Q2.
PhylomeDBi Q9Y5Z9.
TreeFami TF323238.

Enzyme and pathway databases

UniPathwayi UPA00079 .
UPA00232 .

Miscellaneous databases

ChiTaRSi UBIAD1. human.
GeneWikii UBIAD1.
GenomeRNAii 29914.
NextBioi 52502.
PROi Q9Y5Z9.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y5Z9.
CleanExi HS_UBIAD1.
Genevestigatori Q9Y5Z9.

Family and domain databases

InterProi IPR000537. UbiA_prenyltransferase.
IPR026046. UBIAD1.
[Graphical view ]
Pfami PF01040. UbiA. 1 hit.
[Graphical view ]
PIRSFi PIRSF005355. UBIAD1. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of the TERE1 gene, a gene down-regulated in transitional cell carcinoma of the bladder."
    McGarvey T.W., Nguyen T., Tomaszewski J.E., Monson F.C., Malkowicz S.B.
    Oncogene 20:1042-1051(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Tissue: Spleen.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Liver.
  4. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
    Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Lung.
  8. "TERE1, a novel gene affecting growth regulation in prostate carcinoma."
    McGarvey T.W., Nguyen T., Puthiyaveettil R., Tomaszewski J.E., Malkowicz S.B.
    Prostate 54:144-155(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN CARCINOMA, SUBCELLULAR LOCATION.
  9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  10. "Identification of UBIAD1 as a novel human menaquinone-4 biosynthetic enzyme."
    Nakagawa K., Hirota Y., Sawada N., Yuge N., Watanabe M., Uchino Y., Okuda N., Shimomura Y., Suhara Y., Okano T.
    Nature 468:117-121(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PATHWAY, SUBCELLULAR LOCATION.
  11. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Ubiad1 is an antioxidant enzyme that regulates eNOS activity by CoQ10 synthesis."
    Mugoni V., Postel R., Catanzaro V., De Luca E., Turco E., Digilio G., Silengo L., Murphy M.P., Medana C., Stainier D.Y., Bakkers J., Santoro M.M.
    Cell 152:504-518(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS SCCD SER-102 AND GLY-112.
  13. "Mutations in the UBIAD1 gene on chromosome short arm 1, region 36, cause Schnyder crystalline corneal dystrophy."
    Weiss J.S., Kruth H.S., Kuivaniemi H., Tromp G., White P.S., Winters R.S., Lisch W., Henn W., Denninger E., Krause M., Wasson P., Ebenezer N., Mahurkar S., Nickerson M.L.
    Invest. Ophthalmol. Vis. Sci. 48:5007-5012(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS SCCD SER-102 AND ARG-177.
  14. "Mutations in the UBIAD1 gene, encoding a potential prenyltransferase, are causal for Schnyder crystalline corneal dystrophy."
    Orr A., Dube M.-P., Marcadier J., Jiang H., Federico A., George S., Seamone C., Andrews D., Dubord P., Holland S., Provost S., Mongrain V., Evans S., Higgins B., Bowman S., Guernsey D., Samuels M.
    PLoS ONE 2:E685-E685(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS SCCD SER-102; GLY-112; GLY-119; ILE-175 AND SER-232, VARIANT PHE-75.
  15. Cited for: VARIANTS SCCD SER-102; GLY-118; PHE-121; PRO-171; ILE-175; ARG-177; ARG-186 AND GLU-236.
  16. "Surgical management and genetic analysis of a Chinese family with the S171P mutation in the UBIAD1 gene, the gene for Schnyder corneal dystrophy."
    Mehta J.S., Vithana E.N., Venkataraman D., Venkatraman A., Yong V.H., Aung T., Tan D.T.
    Br. J. Ophthalmol. 93:926-931(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SCCD PRO-171.
  17. "A novel UBIAD1 mutation identified in a Chinese family with Schnyder crystalline corneal dystrophy."
    Jing Y., Liu C., Xu J., Wang L.
    Mol. Vis. 15:1463-1469(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SCCD SER-98.
  18. "Newly reported p.Asp240Asn mutation in UBIAD1 suggests central discoid corneal dystrophy is a variant of Schnyder corneal dystrophy."
    Weiss J.S., Wiaux C., Yellore V., Raber I., Eagle R., Mequio M., Aldave A.
    Cornea 29:777-780(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SCCD ASN-240.
  19. Cited for: VARIANTS SCCD THR-97; SER-102; ASN-112; GLY-122; GLU-122 AND HIS-188, SUBCELLULAR LOCATION.
  20. Cited for: VARIANT GLU-177, CHARACTERIZATION OF VARIANTS SCCD SER-102; ASN-112; GLU-177 AND ARG-177, INTERACTION WITH HMGCR AND SOAT1.

Entry informationi

Entry nameiUBIA1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5Z9
Secondary accession number(s): B3KQG3, Q53GX3, Q5THD4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 106 of the entry and version 1 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

Miscellaneous

Strongly down-regulated in transitional cell carcinoma of the bladder and in prostate carcinoma (at protein level) (1 Publication, 1 Publication).

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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

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