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Q9Y5Z9 (UBIA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UbiA prenyltransferase domain-containing protein 1

EC=2.5.1.-
Alternative name(s):
Transitional epithelial response protein 1
Gene names
Name:UBIAD1
Synonyms:TERE1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length338 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Prenyltransferase that mediates the formation of menaquinone-4 (MK-4) and coenzyme Q10. MK-4 is a vitamin K2 isoform presentat 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. Ref.10 Ref.12

Pathway

Cofactor biosynthesis; menaquinone biosynthesis. Ref.10

Cofactor biosynthesis; ubiquinone biosynthesis. Ref.10

Subunit structure

Interacts with HMGCR and SOAT1. Ref.20

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Mitochondrion membrane. Cytoplasm. Nucleus Ref.1 Ref.8 Ref.10 Ref.12 Ref.19.

Tissue specificity

Ubiquitously expressed. Ref.1

Involvement in disease

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. Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20

Miscellaneous

Strongly down-regulated in transitional cell carcinoma of the bladder and in prostate carcinoma (at protein level) (Ref.1, Ref.8).

Sequence similarities

Belongs to the UbiA prenyltransferase family.

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y5Z9-1)

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.
Isoform 2 (identifier: Q9Y5Z9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     177-179: GIG → VLI
     180-338: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 338337UbiA prenyltransferase domain-containing protein 1
PRO_0000242627

Regions

Transmembrane83 – 10321Helical; Potential
Transmembrane134 – 15421Helical; Potential
Transmembrane160 – 18021Helical; Potential
Transmembrane188 – 20821Helical; Potential
Transmembrane209 – 22921Helical; Potential
Transmembrane245 – 26723Helical; Potential
Transmembrane277 – 29721Helical; Potential
Transmembrane315 – 33521Helical; Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.9 Ref.11

Natural variations

Alternative sequence177 – 1793GIG → VLI in isoform 2.
VSP_019455
Alternative sequence180 – 338159Missing in isoform 2.
VSP_019456
Natural variant751S → F. Ref.14
Corresponds to variant rs114000606 [ dbSNP | Ensembl ].
VAR_043713
Natural variant971A → T in SCCD. Ref.19
VAR_064337
Natural variant981G → S in SCCD. Ref.17
VAR_064338
Natural variant1021N → S in SCCD; reduced menaquinone-4 (MK-4) synthesis; does not affect coenzyme Q10 synthesis. Ref.12 Ref.13 Ref.14 Ref.15 Ref.19 Ref.20
VAR_043714
Natural variant1121D → G in SCCD; does not affect coenzyme Q10 synthesis. Ref.12 Ref.14
VAR_043715
Natural variant1121D → N in SCCD; reduced menaquinone-4 (MK-4) synthesis. Ref.19 Ref.20
VAR_064339
Natural variant1181D → G in SCCD. Ref.15
VAR_043716
Natural variant1191R → G in SCCD. Ref.14
VAR_043717
Natural variant1211L → F in SCCD. Ref.15
VAR_043718
Natural variant1221V → E in SCCD. Ref.19
VAR_064340
Natural variant1221V → G in SCCD. Ref.19
VAR_064341
Natural variant1711S → P in SCCD. Ref.15 Ref.16
VAR_043719
Natural variant1751T → I in SCCD. Ref.14 Ref.15
VAR_043720
Natural variant1771G → E in SCCD; reduced menaquinone-4 (MK-4) synthesis. Ref.20
VAR_069267
Natural variant1771G → R in SCCD; reduced menaquinone-4 (MK-4) synthesis. Ref.13 Ref.15 Ref.20
VAR_043721
Natural variant1861G → R in SCCD. Ref.15
VAR_043722
Natural variant1881L → H in SCCD. Ref.19
VAR_064342
Natural variant2321N → S in SCCD. Ref.14
VAR_043723
Natural variant2361D → E in SCCD. Ref.15
VAR_043724
Natural variant2401D → N in SCCD. Ref.18
VAR_064343

Experimental info

Sequence conflict1631I → V in BAD96528. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 02808542DB9EA249

FASTA33836,831
        10         20         30         40         50         60 
MAASQVLGEK INILSGETVK AGDRDPLGND CPEQDRLPQR SWRQKCASYV LALRPWSFSA 

        70         80         90        100        110        120 
SLTPVALGSA LAYRSHGVLD PRLLVGCAVA VLAVHGAGNL VNTYYDFSKG IDHKKSDDRT 

       130        140        150        160        170        180 
LVDRILEPQD VVRFGVFLYT LGCVCAACLY YLSPLKLEHL ALIYFGGLSG SFLYTGGIGF 

       190        200        210        220        230        240 
KYVALGDLII LITFGPLAVM FAYAIQVGSL AIFPLVYAIP LALSTEAILH SNNTRDMESD 

       250        260        270        280        290        300 
REAGIVTLAI LIGPTFSYIL YNTLLFLPYL VFSILATHCT ISLALPLLTI PMAFSLERQF 

       310        320        330 
RSQAFNKLPQ RTAKLNLLLG LFYVFGIILA PAGSLPKI 

« Hide

Isoform 2 [UniParc].

Checksum: 78C76B7F91C92017
Show »

FASTA17919,482

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Genetic analysis of 14 families with Schnyder crystalline corneal dystrophy reveals clues to UBIAD1 protein function."
Weiss J.S., Kruth H.S., Kuivaniemi H., Tromp G., Karkera J., Mahurkar S., Lisch W., Dupps W.J. Jr., White P.S., Winters R.S., Kim C., Rapuano C.J., Sutphin J., Reidy J., Hu F.-R., Lu da W., Ebenezer N., Nickerson M.L.
Am. J. Med. Genet. A 146:271-283(2008) [PubMed] [Europe PMC] [Abstract]
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]"UBIAD1 mutation alters a mitochondrial prenyltransferase to cause Schnyder corneal dystrophy."
Nickerson M.L., Kostiha B.N., Brandt W., Fredericks W., Xu K.P., Yu F.S., Gold B., Chodosh J., Goldberg M., Lu da W., Yamada M., Tervo T.M., Grutzmacher R., Croasdale C., Hoeltzenbein M., Sutphin J., Malkowicz S.B., Wessjohann L. expand/collapse author list , Kruth H.S., Dean M., Weiss J.S.
PLoS ONE 5:E10760-E10760(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SCCD THR-97; SER-102; ASN-112; GLY-122; GLU-122 AND HIS-188, SUBCELLULAR LOCATION.
[20]"The UBIAD1 prenyltransferase links menaquione-4 synthesis to cholesterol metabolic enzymes."
Nickerson M.L., Bosley A.D., Weiss J.S., Kostiha B.N., Hirota Y., Brandt W., Esposito D., Kinoshita S., Wessjohann L., Morham S.G., Andresson T., Kruth H.S., Okano T., Dean M.
Hum. Mutat. 34:317-329(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLU-177, CHARACTERIZATION OF VARIANTS SCCD SER-102; ASN-112; GLU-177 AND ARG-177, INTERACTION WITH HMGCR AND SOAT1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_037451.1. NM_013319.2.
UniGeneHs.522933.

3D structure databases

ProteinModelPortalQ9Y5Z9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118958. 1 interaction.
IntActQ9Y5Z9. 4 interactions.
MINTMINT-3087699.
STRING9606.ENSP00000366006.

PTM databases

PhosphoSiteQ9Y5Z9.

Polymorphism databases

DMDM74753514.

Proteomic databases

PaxDbQ9Y5Z9.
PRIDEQ9Y5Z9.

Protocols and materials databases

DNASU29914.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000376804; ENSP00000366000; ENSG00000120942. [Q9Y5Z9-2]
ENST00000376810; ENSP00000366006; ENSG00000120942. [Q9Y5Z9-1]
GeneID29914.
KEGGhsa:29914.
UCSCuc001asg.3. human. [Q9Y5Z9-1]

Organism-specific databases

CTD29914.
GeneCardsGC01P011334.
HGNCHGNC:30791. UBIAD1.
HPAHPA038200.
HPA044862.
MIM121800. phenotype.
611632. gene.
neXtProtNX_Q9Y5Z9.
Orphanet98967. Schnyder corneal dystrophy.
PharmGKBPA142670660.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1575.
HOGENOMHOG000231452.
HOVERGENHBG080284.
InParanoidQ9Y5Z9.
OMARVTQSGM.
OrthoDBEOG7XH6Q2.
PhylomeDBQ9Y5Z9.
TreeFamTF323238.

Enzyme and pathway databases

UniPathwayUPA00079.
UPA00232.

Gene expression databases

BgeeQ9Y5Z9.
CleanExHS_UBIAD1.
GenevestigatorQ9Y5Z9.

Family and domain databases

InterProIPR000537. UbiA_prenyltransferase.
IPR026046. UBIAD1.
[Graphical view]
PfamPF01040. UbiA. 1 hit.
[Graphical view]
PIRSFPIRSF005355. UBIAD1. 1 hit.
ProtoNetSearch...

Other

ChiTaRSUBIAD1. human.
GeneWikiUBIAD1.
GenomeRNAi29914.
NextBio52502.
PROQ9Y5Z9.
SOURCESearch...

Entry information

Entry nameUBIA1_HUMAN
AccessionPrimary (citable) accession number: Q9Y5Z9
Secondary accession number(s): B3KQG3, Q53GX3, Q5THD4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 103 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

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