Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

O43837

- IDH3B_HUMAN

UniProt

O43837 - IDH3B_HUMAN

Protein

Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial

Gene

IDH3B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 2 (01 May 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

    Isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH.

    Cofactori

    Binds 1 magnesium or manganese ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei133 – 1331SubstrateBy similarity
    Binding sitei164 – 1641SubstrateBy similarity
    Sitei171 – 1711Critical for catalysisBy similarity
    Sitei218 – 2181Critical for catalysisBy similarity
    Metal bindingi251 – 2511Magnesium or manganeseBy similarity
    Binding sitei251 – 2511SubstrateBy similarity

    GO - Molecular functioni

    1. electron carrier activity Source: UniProtKB
    2. isocitrate dehydrogenase (NAD+) activity Source: ProtInc
    3. magnesium ion binding Source: InterPro
    4. NAD binding Source: InterPro

    GO - Biological processi

    1. 2-oxoglutarate metabolic process Source: Ensembl
    2. cellular metabolic process Source: Reactome
    3. isocitrate metabolic process Source: ProtInc
    4. NADH metabolic process Source: Ensembl
    5. small molecule metabolic process Source: Reactome
    6. tricarboxylic acid cycle Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding, NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000101365-MONOMER.
    ReactomeiREACT_1785. Citric acid cycle (TCA cycle).
    SABIO-RKO43837.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial (EC:1.1.1.41)
    Alternative name(s):
    Isocitric dehydrogenase subunit beta
    NAD(+)-specific ICDH subunit beta
    Gene namesi
    Name:IDH3B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:5385. IDH3B.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: Reactome
    2. mitochondrion Source: HPA
    3. nucleus Source: UniProt

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Retinitis pigmentosa 46 (RP46) [MIM:612572]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti132 – 1321L → P in RP46. 1 Publication
    VAR_054851

    Keywords - Diseasei

    Disease mutation, Retinitis pigmentosa

    Organism-specific databases

    MIMi612572. phenotype.
    Orphaneti791. Retinitis pigmentosa.
    PharmGKBiPA29633.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3434MitochondrionBy similarityAdd
    BLAST
    Chaini35 – 385351Isocitrate dehydrogenase [NAD] subunit beta, mitochondrialPRO_0000014444Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei199 – 1991N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO43837.
    PaxDbiO43837.
    PRIDEiO43837.

    PTM databases

    PhosphoSiteiO43837.

    Expressioni

    Gene expression databases

    ArrayExpressiO43837.
    BgeeiO43837.
    CleanExiHS_IDH3B.
    GenevestigatoriO43837.

    Organism-specific databases

    HPAiHPA049387.
    HPA054180.

    Interactioni

    Subunit structurei

    Heterooligomer of subunits alpha, beta, and gamma in the apparent ratio of 2:1:1.By similarity

    Protein-protein interaction databases

    BioGridi109646. 7 interactions.
    IntActiO43837. 6 interactions.
    MINTiMINT-5003855.
    STRINGi9606.ENSP00000370223.

    Structurei

    3D structure databases

    ProteinModelPortaliO43837.
    SMRiO43837. Positions 47-382.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0473.
    HOVERGENiHBG052080.
    InParanoidiO43837.
    KOiK00030.
    OMAiILATPDY.
    OrthoDBiEOG75B85R.
    PhylomeDBiO43837.
    TreeFamiTF315033.

    Family and domain databases

    Gene3Di3.40.718.10. 1 hit.
    InterProiIPR019818. IsoCit/isopropylmalate_DH_CS.
    IPR001804. Isocitrate/isopropylmalate_DH.
    IPR004434. Isocitrate_DH_NAD.
    IPR024084. IsoPropMal-DH-like_dom.
    [Graphical view]
    PANTHERiPTHR11835. PTHR11835. 1 hit.
    PfamiPF00180. Iso_dh. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00175. mito_nad_idh. 1 hit.
    PROSITEiPS00470. IDH_IMDH. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform B (identifier: O43837-1) [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

    MAALSGVRWL TRALVSAGNP GAWRGLSTSA AAHAASRSQA EDVRVEGSFP    50
    VTMLPGDGVG PELMHAVKEV FKAAAVPVEF QEHHLSEVQN MASEEKLEQV 100
    LSSMKENKVA IIGKIHTPME YKGELASYDM RLRRKLDLFA NVVHVKSLPG 150
    YMTRHNNLDL VIIREQTEGE YSSLEHESAR GVIECLKIVT RAKSQRIAKF 200
    AFDYATKKGR GKVTAVHKAN IMKLGDGLFL QCCEEVAELY PKIKFETMII 250
    DNCCMQLVQN PYQFDVLVMP NLYGNIIDNL AAGLVGGAGV VPGESYSAEY 300
    AVFETGARHP FAQAVGRNIA NPTAMLLSAS NMLRHLNLEY HSSMIADAVK 350
    KVIKVGKVRT RDMGGYSTTT DFIKSVIGHL QTKGS 385
    Length:385
    Mass (Da):42,184
    Last modified:May 1, 2007 - v2
    Checksum:i7324E6CC30A68EE2
    GO
    Isoform A (identifier: O43837-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         361-385: RDMGGYSTTTDFIKSVIGHLQTKGS → SDMGGYATCHDFTEAVIAALPHP

    Show »
    Length:383
    Mass (Da):41,887
    Checksum:i6B5A3D3F82CCDB34
    GO
    Isoform C (identifier: O43837-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-177: MAALSGVRWL...EGEYSSLEHE → MKMGERWSSLFPFPVSPSCCFLLTQ

    Show »
    Length:233
    Mass (Da):25,555
    Checksum:i7036C0A641A17E2D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti127 – 1304SYDM → RTLV in CAB43266. (PubMed:17974005)Curated
    Sequence conflicti250 – 2501I → V in BAA91971. (PubMed:14702039)Curated
    Sequence conflicti385 – 3851S → SNL in AAD09340. (PubMed:10601238)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti3 – 31A → V.1 Publication
    Corresponds to variant rs3178817 [ dbSNP | Ensembl ].
    VAR_022660
    Natural varianti132 – 1321L → P in RP46. 1 Publication
    VAR_054851
    Natural varianti166 – 1661Q → H.
    Corresponds to variant rs11542741 [ dbSNP | Ensembl ].
    VAR_049781
    Natural varianti360 – 3601T → A.
    Corresponds to variant rs8296 [ dbSNP | Ensembl ].
    VAR_056005

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 177177MAALS…SLEHE → MKMGERWSSLFPFPVSPSCC FLLTQ in isoform C. 1 PublicationVSP_041335Add
    BLAST
    Alternative sequencei361 – 38525RDMGG…QTKGS → SDMGGYATCHDFTEAVIAAL PHP in isoform A. 1 PublicationVSP_002462Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U49283 mRNA. Translation: AAB94295.1.
    AF023265 mRNA. Translation: AAD09339.1.
    AF023266 mRNA. Translation: AAD09340.1.
    AK001905 mRNA. Translation: BAA91971.1.
    AK315641 mRNA. Translation: BAG38008.1.
    AL049712 Genomic DNA. Translation: CAC01442.2.
    AL049712 Genomic DNA. Translation: CAC01443.1.
    CH471133 Genomic DNA. Translation: EAX10579.1.
    CH471133 Genomic DNA. Translation: EAX10580.1.
    CH471133 Genomic DNA. Translation: EAX10582.1.
    CH471133 Genomic DNA. Translation: EAX10583.1.
    BC001960 mRNA. Translation: AAH01960.1.
    AL050094 mRNA. Translation: CAB43266.1.
    CCDSiCCDS13031.1. [O43837-2]
    CCDS13032.1. [O43837-1]
    PIRiT08743.
    T13147.
    RefSeqiNP_008830.2. NM_006899.3. [O43837-1]
    NP_777280.1. NM_174855.2. [O43837-2]
    UniGeneiHs.436405.

    Genome annotation databases

    EnsembliENST00000380843; ENSP00000370223; ENSG00000101365. [O43837-1]
    ENST00000380851; ENSP00000370232; ENSG00000101365. [O43837-2]
    GeneIDi3420.
    KEGGihsa:3420.
    UCSCiuc002wgp.4. human. [O43837-1]
    uc002wgq.4. human. [O43837-2]
    uc002wgr.4. human. [O43837-3]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U49283 mRNA. Translation: AAB94295.1 .
    AF023265 mRNA. Translation: AAD09339.1 .
    AF023266 mRNA. Translation: AAD09340.1 .
    AK001905 mRNA. Translation: BAA91971.1 .
    AK315641 mRNA. Translation: BAG38008.1 .
    AL049712 Genomic DNA. Translation: CAC01442.2 .
    AL049712 Genomic DNA. Translation: CAC01443.1 .
    CH471133 Genomic DNA. Translation: EAX10579.1 .
    CH471133 Genomic DNA. Translation: EAX10580.1 .
    CH471133 Genomic DNA. Translation: EAX10582.1 .
    CH471133 Genomic DNA. Translation: EAX10583.1 .
    BC001960 mRNA. Translation: AAH01960.1 .
    AL050094 mRNA. Translation: CAB43266.1 .
    CCDSi CCDS13031.1. [O43837-2 ]
    CCDS13032.1. [O43837-1 ]
    PIRi T08743.
    T13147.
    RefSeqi NP_008830.2. NM_006899.3. [O43837-1 ]
    NP_777280.1. NM_174855.2. [O43837-2 ]
    UniGenei Hs.436405.

    3D structure databases

    ProteinModelPortali O43837.
    SMRi O43837. Positions 47-382.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109646. 7 interactions.
    IntActi O43837. 6 interactions.
    MINTi MINT-5003855.
    STRINGi 9606.ENSP00000370223.

    Chemistry

    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei O43837.

    Proteomic databases

    MaxQBi O43837.
    PaxDbi O43837.
    PRIDEi O43837.

    Protocols and materials databases

    DNASUi 3420.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000380843 ; ENSP00000370223 ; ENSG00000101365 . [O43837-1 ]
    ENST00000380851 ; ENSP00000370232 ; ENSG00000101365 . [O43837-2 ]
    GeneIDi 3420.
    KEGGi hsa:3420.
    UCSCi uc002wgp.4. human. [O43837-1 ]
    uc002wgq.4. human. [O43837-2 ]
    uc002wgr.4. human. [O43837-3 ]

    Organism-specific databases

    CTDi 3420.
    GeneCardsi GC20M002639.
    GeneReviewsi IDH3B.
    HGNCi HGNC:5385. IDH3B.
    HPAi HPA049387.
    HPA054180.
    MIMi 604526. gene.
    612572. phenotype.
    neXtProti NX_O43837.
    Orphaneti 791. Retinitis pigmentosa.
    PharmGKBi PA29633.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0473.
    HOVERGENi HBG052080.
    InParanoidi O43837.
    KOi K00030.
    OMAi ILATPDY.
    OrthoDBi EOG75B85R.
    PhylomeDBi O43837.
    TreeFami TF315033.

    Enzyme and pathway databases

    BioCyci MetaCyc:ENSG00000101365-MONOMER.
    Reactomei REACT_1785. Citric acid cycle (TCA cycle).
    SABIO-RK O43837.

    Miscellaneous databases

    ChiTaRSi IDH3B. human.
    GeneWikii IDH3B.
    GenomeRNAii 3420.
    NextBioi 13482.
    PROi O43837.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43837.
    Bgeei O43837.
    CleanExi HS_IDH3B.
    Genevestigatori O43837.

    Family and domain databases

    Gene3Di 3.40.718.10. 1 hit.
    InterProi IPR019818. IsoCit/isopropylmalate_DH_CS.
    IPR001804. Isocitrate/isopropylmalate_DH.
    IPR004434. Isocitrate_DH_NAD.
    IPR024084. IsoPropMal-DH-like_dom.
    [Graphical view ]
    PANTHERi PTHR11835. PTHR11835. 1 hit.
    Pfami PF00180. Iso_dh. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00175. mito_nad_idh. 1 hit.
    PROSITEi PS00470. IDH_IMDH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and functional characterization of a novel, tissue-specific NAD+-dependent isocitrate dehydrogenase beta subunit isoform."
      Kim Y.-O., Koh H.-J., Kim S.-H., Jo S.-H., Huh J.-W., Jeong K.-S., Lee I.J., Song B.J., Huh T.-L.
      J. Biol. Chem. 274:36866-36875(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), VARIANT VAL-3, ALTERNATIVE SPLICING.
      Tissue: Heart.
    2. "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] (ISOFORMS B AND C).
      Tissue: Placenta and Synovium.
    3. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. 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 B).
      Tissue: Lung.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-385 (ISOFORM B).
      Tissue: Uterus.
    7. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Insights from retinitis pigmentosa into the roles of isocitrate dehydrogenases in the Krebs cycle."
      Hartong D.T., Dange M., McGee T.L., Berson E.L., Dryja T.P., Colman R.F.
      Nat. Genet. 40:1230-1234(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT RP46 PRO-132.

    Entry informationi

    Entry nameiIDH3B_HUMAN
    AccessioniPrimary (citable) accession number: O43837
    Secondary accession number(s): B2RDR1
    , D3DVX2, D3DVX3, O95106, Q5JXS8, Q9NQ06, Q9NQ07, Q9NUZ0, Q9UEX0, Q9UG99
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 151 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 20
      Human chromosome 20: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3