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Q9UBK9

- UXT_HUMAN

UniProt

Q9UBK9 - UXT_HUMAN

Protein

Protein UXT

Gene

UXT

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

    Involved in gene transcription regulation. Acts in concert with the corepressor URI1 to regulate androgen receptor transcription (AR). AR N-terminus-associated coactivator which may play a role in facilitating receptor-induced transcriptional activation (PubMed:11854421). Potential component of mitochondrial-associated LRPPRC, a multidomain organizer that potentially integrates mitochondria and the microtubular cytoskeleton with chromosome remodeling (PubMed:11827465). Increasing concentrations of UXT contributes to progressive aggregation of mitochondria and cell death potentially through its association with LRPPRC (PubMed:17554592). May be a nuclear chaperone that promotes formation of the NF-kappa-B enhanceosome and which is essential for its nuclear function (PubMed:17620405). Suppresses cell transformation and it might mediate this function by interaction and inhibition of the biological activity of cell proliferation and survival stimulatory factors like MECOM (PubMed:17635584). Together with URI1, associates with chromatin to the NKX3-1 promoter region.7 Publications

    GO - Molecular functioni

    1. beta-tubulin binding Source: HGNC
    2. chromatin binding Source: UniProtKB
    3. microtubule binding Source: HGNC
    4. protein binding Source: UniProtKB
    5. RNA polymerase II transcription corepressor activity Source: UniProtKB

    GO - Biological processi

    1. centrosome organization Source: HGNC
    2. microtubule cytoskeleton organization Source: HGNC
    3. mitochondrion transport along microtubule Source: HGNC
    4. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    5. protein folding Source: InterPro

    Keywords - Molecular functioni

    Activator, Chaperone, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein UXT
    Alternative name(s):
    Androgen receptor trapped clone 27 protein
    Short name:
    ART-27
    Ubiquitously expressed transcript protein
    Gene namesi
    Name:UXT
    ORF Names:HSPC024
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:12641. UXT.

    Subcellular locationi

    GO - Cellular componenti

    1. centrosome Source: HGNC
    2. cytoplasm Source: UniProtKB
    3. cytoskeleton Source: HGNC
    4. microtubule organizing center Source: HPA
    5. nucleus Source: UniProtKB
    6. prefoldin complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi50 – 501L → P: Causes dislocation from the centrosome; when associated with L-59. 1 Publication
    Mutagenesisi59 – 591L → P: Causes dislocation from the centrosome; when associated with L-50. 1 Publication

    Organism-specific databases

    PharmGKBiPA37265.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 157157Protein UXTPRO_0000065751Add
    BLAST

    Proteomic databases

    MaxQBiQ9UBK9.
    PaxDbiQ9UBK9.
    PRIDEiQ9UBK9.

    PTM databases

    PhosphoSiteiQ9UBK9.

    Expressioni

    Tissue specificityi

    Ubiquitous. Expressed in prostate epithelial cells. Overexpressed in a number of tumor tissues (PubMed:16221885). Highest levels in the heart, skeletal muscle, pancreas, kidney, liver, adrenal gland, peripheral blood leukocytes, lymph node, prostate, and thyroid and the lowest levels in bladder and uterus.4 Publications

    Gene expression databases

    BgeeiQ9UBK9.
    CleanExiHS_UXT.
    GenevestigatoriQ9UBK9.

    Organism-specific databases

    HPAiHPA050499.
    HPA058400.

    Interactioni

    Subunit structurei

    Homohexamer. Interacts with LRPPRC. Interacts with AR N-terminus. In the nucleus interacts specifically with RELA and forms a dynamic complex with NF-kappa-B and is recruited to the NF-kappa-B enhanceosome upon stimulation. Interacts with MECOM and URI1.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MECOMQ031125EBI-357355,EBI-1384862
    RELAQ042065EBI-357355,EBI-73886
    RPAP3Q9H6T32EBI-357355,EBI-356928
    SARM1Q0D2N82EBI-357355,EBI-8716526

    Protein-protein interaction databases

    BioGridi113997. 15 interactions.
    IntActiQ9UBK9. 27 interactions.
    MINTiMINT-1143575.
    STRINGi9606.ENSP00000337393.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UBK9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the UXT family.Curated

    Phylogenomic databases

    eggNOGiNOG263764.
    HOGENOMiHOG000005748.
    HOVERGENiHBG001087.
    InParanoidiQ9UBK9.
    OrthoDBiEOG7T7GW2.
    PhylomeDBiQ9UBK9.
    TreeFamiTF323827.

    Family and domain databases

    Gene3Di1.10.287.370. 1 hit.
    InterProiIPR003994. PFD_UXT.
    IPR009053. Prefoldin.
    IPR004127. Prefoldin_subunit_alpha.
    [Graphical view]
    PfamiPF02996. Prefoldin. 1 hit.
    [Graphical view]
    PRINTSiPR01502. UXTPROTEIN.
    SUPFAMiSSF46579. SSF46579. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9UBK9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATPPKRRAV EATGEKVLRY ETFISDVLQR DLRKVLDHRD KVYEQLAKYL    50
    QLRNVIERLQ EAKHSELYMQ VDLGCNFFVD TVVPDTSRIY VALGYGFFLE 100
    LTLAEALKFI DRKSSLLTEL SNSLTKDSMN IKAHIHMLLE GLRELQGLQN 150
    FPEKPHH 157
    Length:157
    Mass (Da):18,246
    Last modified:May 1, 2000 - v1
    Checksum:i94CE14C462DEE308
    GO

    Sequence cautioni

    The sequence AAD39840.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAI42447.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF092737 mRNA. Translation: AAD28698.1.
    AF083241 mRNA. Translation: AAD39839.1.
    AF083242 mRNA. Translation: AAD39840.1. Different initiation.
    AL009172 Genomic DNA. Translation: CAI42447.1. Different initiation.
    AL009172 Genomic DNA. Translation: CAI42448.1.
    AK312072 mRNA. Translation: BAG35008.1.
    CH471164 Genomic DNA. Translation: EAW59326.1.
    BC000720 mRNA. Translation: AAH00720.1.
    BC008890 mRNA. Translation: AAH08890.1.
    CCDSiCCDS14285.1.
    RefSeqiNP_004173.1. NM_004182.3.
    NP_705582.1. NM_153477.2.
    UniGeneiHs.172791.
    Hs.735566.

    Genome annotation databases

    EnsembliENST00000333119; ENSP00000327797; ENSG00000126756.
    ENST00000335890; ENSP00000337393; ENSG00000126756.
    GeneIDi8409.
    KEGGihsa:8409.
    UCSCiuc004dim.3. human.

    Polymorphism databases

    DMDMi8928445.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF092737 mRNA. Translation: AAD28698.1 .
    AF083241 mRNA. Translation: AAD39839.1 .
    AF083242 mRNA. Translation: AAD39840.1 . Different initiation.
    AL009172 Genomic DNA. Translation: CAI42447.1 . Different initiation.
    AL009172 Genomic DNA. Translation: CAI42448.1 .
    AK312072 mRNA. Translation: BAG35008.1 .
    CH471164 Genomic DNA. Translation: EAW59326.1 .
    BC000720 mRNA. Translation: AAH00720.1 .
    BC008890 mRNA. Translation: AAH08890.1 .
    CCDSi CCDS14285.1.
    RefSeqi NP_004173.1. NM_004182.3.
    NP_705582.1. NM_153477.2.
    UniGenei Hs.172791.
    Hs.735566.

    3D structure databases

    ProteinModelPortali Q9UBK9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113997. 15 interactions.
    IntActi Q9UBK9. 27 interactions.
    MINTi MINT-1143575.
    STRINGi 9606.ENSP00000337393.

    PTM databases

    PhosphoSitei Q9UBK9.

    Polymorphism databases

    DMDMi 8928445.

    Proteomic databases

    MaxQBi Q9UBK9.
    PaxDbi Q9UBK9.
    PRIDEi Q9UBK9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000333119 ; ENSP00000327797 ; ENSG00000126756 .
    ENST00000335890 ; ENSP00000337393 ; ENSG00000126756 .
    GeneIDi 8409.
    KEGGi hsa:8409.
    UCSCi uc004dim.3. human.

    Organism-specific databases

    CTDi 8409.
    GeneCardsi GC0XM047511.
    HGNCi HGNC:12641. UXT.
    HPAi HPA050499.
    HPA058400.
    MIMi 300234. gene.
    neXtProti NX_Q9UBK9.
    PharmGKBi PA37265.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG263764.
    HOGENOMi HOG000005748.
    HOVERGENi HBG001087.
    InParanoidi Q9UBK9.
    OrthoDBi EOG7T7GW2.
    PhylomeDBi Q9UBK9.
    TreeFami TF323827.

    Miscellaneous databases

    GeneWikii UXT.
    GenomeRNAii 8409.
    NextBioi 31482.
    PROi Q9UBK9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9UBK9.
    CleanExi HS_UXT.
    Genevestigatori Q9UBK9.

    Family and domain databases

    Gene3Di 1.10.287.370. 1 hit.
    InterProi IPR003994. PFD_UXT.
    IPR009053. Prefoldin.
    IPR004127. Prefoldin_subunit_alpha.
    [Graphical view ]
    Pfami PF02996. Prefoldin. 1 hit.
    [Graphical view ]
    PRINTSi PR01502. UXTPROTEIN.
    SUPFAMi SSF46579. SSF46579. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of UXT, a novel gene in human Xp11, which is widely and abundantly expressed in tumor tissue."
      Schroer A., Schneider S., Ropers H.-H., Nothwang H.G.
      Genomics 56:340-343(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Identification and characterization of ART-27, a novel coactivator for the androgen receptor N terminus."
      Markus S.M., Taneja S.S., Logan S.K., Li W., Ha S., Hittelman A.B., Rogatsky I., Garabedian M.J.
      Mol. Biol. Cell 13:670-682(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH AR.
    3. "UXT interacts with the transcriptional repressor protein EVI1 and suppresses cell transformation."
      McGilvray R., Walker M., Bartholomew C.
      FEBS J. 274:3960-3971(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH MECOM.
    4. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Umbilical cord blood.
    5. Zhou J., Ye M., Fu G., Zhang Q., Shen Y., Huang Q., Xu S., He K., Chen S., Mao M., Chen Z.
      Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Umbilical cord blood.
    6. "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].
      Tissue: Mammary gland.
    7. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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: Placenta.
    10. "Sequence analysis of LRPPRC and its SEC1 domain interaction partners suggests roles in cytoskeletal organization, vesicular trafficking, nucleocytosolic shuttling, and chromosome activity."
      Liu L., McKeehan W.L.
      Genomics 79:124-136(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH LRPPRC.
    11. "UXT is a novel centrosomal protein essential for cell viability."
      Zhao H., Wang Q., Zhang H., Liu Q., Du X., Richter M., Greene M.I.
      Mol. Biol. Cell 16:5857-5865(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, HOMOHEXAMERIZATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-50 AND LEU-59.
    12. "UXT (Ubiquitously Expressed Transcript) causes mitochondrial aggregation."
      Moss T.N., Vo A., McKeehan W.L., Liu L.
      In Vitro Cell. Dev. Biol. Anim. 43:139-146(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "UXT is a novel and essential cofactor in the NF-kappaB transcriptional enhanceosome."
      Sun S., Tang Y., Lou X., Zhu L., Yang K., Zhang B., Shi H., Wang C.
      J. Cell Biol. 178:231-244(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RELA.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: FUNCTION, INTERACTION WITH URI1, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiUXT_HUMAN
    AccessioniPrimary (citable) accession number: Q9UBK9
    Secondary accession number(s): B2R561, Q5JZG3, Q9Y6E5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 114 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3