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P56693

- SOX10_HUMAN

UniProt

P56693 - SOX10_HUMAN

Protein

Transcription factor SOX-10

Gene

SOX10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 1 (15 Jul 1999)
      Previous versions | rss
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    Functioni

    Transcription factor that seems to function synergistically with the POU domain protein TST-1/OCT6/SCIP. Could confer cell specificity to the function of other transcription factors in developing and mature glia By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi104 – 17269HMG boxPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: Ensembl
    2. identical protein binding Source: IntAct
    3. protein binding Source: IntAct
    4. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
    5. RNA polymerase II distal enhancer sequence-specific DNA binding Source: Ensembl
    6. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: Ensembl
    7. RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
    8. transcription coactivator activity Source: ProtInc

    GO - Biological processi

    1. anatomical structure morphogenesis Source: ProtInc
    2. cell maturation Source: Ensembl
    3. developmental growth Source: Ensembl
    4. digestive tract morphogenesis Source: Ensembl
    5. enteric nervous system development Source: Ensembl
    6. in utero embryonic development Source: Ensembl
    7. melanocyte differentiation Source: Ensembl
    8. negative regulation of apoptotic process Source: Ensembl
    9. negative regulation of canonical Wnt signaling pathway Source: Ensembl
    10. negative regulation of transcription, DNA-templated Source: Ensembl
    11. neural crest cell migration Source: Ensembl
    12. oligodendrocyte differentiation Source: Ensembl
    13. peripheral nervous system development Source: Ensembl
    14. positive regulation of gliogenesis Source: Ensembl
    15. positive regulation of neuroblast proliferation Source: Ensembl
    16. regulation of transcription from RNA polymerase II promoter Source: ProtInc

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    SignaLinkiP56693.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription factor SOX-10
    Gene namesi
    Name:SOX10
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:11190. SOX10.

    Subcellular locationi

    GO - Cellular componenti

    1. extrinsic component of mitochondrial outer membrane Source: Ensembl
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Waardenburg syndrome 2E (WS2E) [MIM:611584]: An autosomal dominant auditory-pigmentary disorder characterized by sensorineural deafness, pigmentary disturbances of the hair, skin and eyes, and absence of dystopia canthorum which is the lateral displacement of the inner canthus of each eye. Individuals with WS2E may have neurologic abnormalities, including mental impairment, myelination defects, and ataxia. Some patients can manifest features of Kallmann syndrome.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti112 – 1121M → I in WS2E and PCWH; increased DNA binding capacity. 1 Publication
    VAR_066748
    Natural varianti135 – 1351S → T in WS2E; without neurologic involvement. 1 Publication
    VAR_021386
    Natural varianti161 – 1611R → H in WS2E; reduced DNA binding capacity. 1 Publication
    VAR_066753
    Waardenburg syndrome 4C (WS4C) [MIM:613266]: A disorder characterized by the association of Waardenburg features (depigmentation and deafness) with the absence of enteric ganglia in the distal part of the intestine (Hirschsprung disease).3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti106 – 1061R → W in WS4C; loss of DNA binding and transactivation capacity. 1 Publication
    VAR_066747
    Natural varianti145 – 1451L → P in WS4C; loss of DNA binding and transactivation capacity. 1 Publication
    VAR_066750
    Natural varianti157 – 1571A → V in WS4C; loss of DNA binding and transactivation capacity. 2 Publications
    VAR_066752
    Natural varianti161 – 1611R → RLR in WS4C. 1 Publication
    VAR_003743
    Peripheral demyelinating neuropathy, central dysmyelinating leukodystrophy, Waardenburg syndrome and Hirschsprung disease (PCWH) [MIM:609136]: A complex neurocristopathy that includes features of 4 distinct syndromes: peripheral demyelinating neuropathy, central dysmyelinating leukodystrophy, Waardenburg syndrome and Hirschsprung disease.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti112 – 1121M → I in WS2E and PCWH; increased DNA binding capacity. 1 Publication
    VAR_066748
    Natural varianti131 – 1311N → H in PCWH; reduced DNA binding capacity. 1 Publication
    VAR_066749
    Natural varianti150 – 1501K → N in PCWH; loss of DNA binding and transactivation capacity. 1 Publication
    VAR_066751
    Natural varianti174 – 1741Q → P in PCWH; without Hirschsprung disease; reduced DNA binding capacity. 2 Publications
    VAR_066754
    Natural varianti175 – 1751P → A in PCWH; reduced DNA binding capacity. 1 Publication
    VAR_066755
    Natural varianti175 – 1751P → L in PCWH; reduced DNA binding capacity. 1 Publication
    VAR_066756
    Natural varianti175 – 1751P → R in PCWH; reduced DNA binding capacity. 1 Publication
    VAR_066757
    Natural varianti321 – 3211G → R in PCWH. 1 Publication
    VAR_066758

    Keywords - Diseasei

    Deafness, Disease mutation, Hirschsprung disease, Kallmann syndrome, Waardenburg syndrome

    Organism-specific databases

    MIMi609136. phenotype.
    611584. phenotype.
    613266. phenotype.
    Orphaneti478. Kallmann syndrome.
    163746. Neurologic Waardenburg-Shah syndrome.
    895. Waardenburg syndrome type 2.
    897. Waardenburg-Shah syndrome.
    PharmGKBiPA36027.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 466466Transcription factor SOX-10PRO_0000048746Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei24 – 241Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP56693.
    PRIDEiP56693.

    PTM databases

    PhosphoSiteiP56693.

    Expressioni

    Tissue specificityi

    Expressed in fetal brain and in adult brain, heart, small intestine and colon.

    Gene expression databases

    ArrayExpressiP56693.
    BgeeiP56693.
    CleanExiHS_SOX10.
    GenevestigatoriP56693.

    Organism-specific databases

    HPAiCAB003171.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-1167533,EBI-1167533
    NMIQ132872EBI-1167533,EBI-372942
    PAX3P237602EBI-1167533,EBI-1167564
    POU3F2P202653EBI-1167533,EBI-1167176
    SUMO1P631652EBI-1167533,EBI-80140
    UBE2IP632792EBI-1167533,EBI-80168

    Protein-protein interaction databases

    BioGridi112546. 7 interactions.
    IntActiP56693. 7 interactions.
    MINTiMINT-1781695.
    STRINGi9606.ENSP00000354130.

    Structurei

    3D structure databases

    ProteinModelPortaliP56693.
    SMRiP56693. Positions 102-173.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi134 – 14512Nuclear export signalAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi35 – 417Poly-Gly

    Sequence similaritiesi

    Contains 1 HMG box DNA-binding domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG295709.
    HOGENOMiHOG000108876.
    HOVERGENiHBG002061.
    InParanoidiP56693.
    KOiK09270.
    OMAiPYYGHSS.
    PhylomeDBiP56693.

    Family and domain databases

    Gene3Di1.10.30.10. 1 hit.
    InterProiIPR009071. HMG_box_dom.
    IPR022151. Sox_N.
    [Graphical view]
    PfamiPF00505. HMG_box. 1 hit.
    PF12444. Sox_N. 1 hit.
    [Graphical view]
    SMARTiSM00398. HMG. 1 hit.
    [Graphical view]
    SUPFAMiSSF47095. SSF47095. 1 hit.
    PROSITEiPS50118. HMG_BOX_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P56693-1) [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

    MAEEQDLSEV ELSPVGSEEP RCLSPGSAPS LGPDGGGGGS GLRASPGPGE    50
    LGKVKKEQQD GEADDDKFPV CIREAVSQVL SGYDWTLVPM PVRVNGASKS 100
    KPHVKRPMNA FMVWAQAARR KLADQYPHLH NAELSKTLGK LWRLLNESDK 150
    RPFIEEAERL RMQHKKDHPD YKYQPRRRKN GKAAQGEAEC PGGEAEQGGT 200
    AAIQAHYKSA HLDHRHPGEG SPMSDGNPEH PSGQSHGPPT PPTTPKTELQ 250
    SGKADPKRDG RSMGEGGKPH IDFGNVDIGE ISHEVMSNME TFDVAELDQY 300
    LPPNGHPGHV SSYSAAGYGL GSALAVASGH SAWISKPPGV ALPTVSPPGV 350
    DAKAQVKTET AGPQGPPHYT DQPSTSQIAY TSLSLPHYGS AFPSISRPQF 400
    DYSDHQPSGP YYGHSGQASG LYSAFSYMGP SQRPLYTAIS DPSPSGPQSH 450
    SPTHWEQPVY TTLSRP 466
    Length:466
    Mass (Da):49,911
    Last modified:July 15, 1999 - v1
    Checksum:iFAA1EC108D4DE6A1
    GO
    Isoform 2 (identifier: P56693-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         262-441: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:286
    Mass (Da):31,088
    Checksum:i164087BF740FF550
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti222 – 2221P → L in CAG38808. 1 PublicationCurated
    Sequence conflicti461 – 4611T → M in CAG38808. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti106 – 1061R → W in WS4C; loss of DNA binding and transactivation capacity. 1 Publication
    VAR_066747
    Natural varianti112 – 1121M → I in WS2E and PCWH; increased DNA binding capacity. 1 Publication
    VAR_066748
    Natural varianti131 – 1311N → H in PCWH; reduced DNA binding capacity. 1 Publication
    VAR_066749
    Natural varianti135 – 1351S → T in WS2E; without neurologic involvement. 1 Publication
    VAR_021386
    Natural varianti145 – 1451L → P in WS4C; loss of DNA binding and transactivation capacity. 1 Publication
    VAR_066750
    Natural varianti150 – 1501K → N in PCWH; loss of DNA binding and transactivation capacity. 1 Publication
    VAR_066751
    Natural varianti157 – 1571A → V in WS4C; loss of DNA binding and transactivation capacity. 2 Publications
    VAR_066752
    Natural varianti161 – 1611R → H in WS2E; reduced DNA binding capacity. 1 Publication
    VAR_066753
    Natural varianti161 – 1611R → RLR in WS4C. 1 Publication
    VAR_003743
    Natural varianti174 – 1741Q → P in PCWH; without Hirschsprung disease; reduced DNA binding capacity. 2 Publications
    VAR_066754
    Natural varianti175 – 1751P → A in PCWH; reduced DNA binding capacity. 1 Publication
    VAR_066755
    Natural varianti175 – 1751P → L in PCWH; reduced DNA binding capacity. 1 Publication
    VAR_066756
    Natural varianti175 – 1751P → R in PCWH; reduced DNA binding capacity. 1 Publication
    VAR_066757
    Natural varianti321 – 3211G → R in PCWH. 1 Publication
    VAR_066758

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei262 – 441180Missing in isoform 2. 1 PublicationVSP_053874Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ001183 mRNA. Translation: CAA04576.1.
    CR456584 mRNA. Translation: CAG30470.1.
    BT020029 mRNA. Translation: AAV38832.1.
    AK300945 mRNA. Translation: BAG62574.1.
    CR536571 mRNA. Translation: CAG38808.1.
    AL031587 Genomic DNA. Translation: CAB62982.1.
    BC002824 mRNA. Translation: AAH02824.1.
    BC007595 mRNA. Translation: AAH07595.1.
    CCDSiCCDS13964.1. [P56693-1]
    RefSeqiNP_008872.1. NM_006941.3. [P56693-1]
    UniGeneiHs.376984.

    Genome annotation databases

    EnsembliENST00000360880; ENSP00000354130; ENSG00000100146. [P56693-1]
    ENST00000396884; ENSP00000380093; ENSG00000100146. [P56693-1]
    GeneIDi6663.
    KEGGihsa:6663.
    UCSCiuc003aun.1. human. [P56693-1]

    Polymorphism databases

    DMDMi6175075.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ001183 mRNA. Translation: CAA04576.1 .
    CR456584 mRNA. Translation: CAG30470.1 .
    BT020029 mRNA. Translation: AAV38832.1 .
    AK300945 mRNA. Translation: BAG62574.1 .
    CR536571 mRNA. Translation: CAG38808.1 .
    AL031587 Genomic DNA. Translation: CAB62982.1 .
    BC002824 mRNA. Translation: AAH02824.1 .
    BC007595 mRNA. Translation: AAH07595.1 .
    CCDSi CCDS13964.1. [P56693-1 ]
    RefSeqi NP_008872.1. NM_006941.3. [P56693-1 ]
    UniGenei Hs.376984.

    3D structure databases

    ProteinModelPortali P56693.
    SMRi P56693. Positions 102-173.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112546. 7 interactions.
    IntActi P56693. 7 interactions.
    MINTi MINT-1781695.
    STRINGi 9606.ENSP00000354130.

    PTM databases

    PhosphoSitei P56693.

    Polymorphism databases

    DMDMi 6175075.

    Proteomic databases

    PaxDbi P56693.
    PRIDEi P56693.

    Protocols and materials databases

    DNASUi 6663.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360880 ; ENSP00000354130 ; ENSG00000100146 . [P56693-1 ]
    ENST00000396884 ; ENSP00000380093 ; ENSG00000100146 . [P56693-1 ]
    GeneIDi 6663.
    KEGGi hsa:6663.
    UCSCi uc003aun.1. human. [P56693-1 ]

    Organism-specific databases

    CTDi 6663.
    GeneCardsi GC22M038366.
    HGNCi HGNC:11190. SOX10.
    HPAi CAB003171.
    MIMi 602229. gene.
    609136. phenotype.
    611584. phenotype.
    613266. phenotype.
    neXtProti NX_P56693.
    Orphaneti 478. Kallmann syndrome.
    163746. Neurologic Waardenburg-Shah syndrome.
    895. Waardenburg syndrome type 2.
    897. Waardenburg-Shah syndrome.
    PharmGKBi PA36027.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG295709.
    HOGENOMi HOG000108876.
    HOVERGENi HBG002061.
    InParanoidi P56693.
    KOi K09270.
    OMAi PYYGHSS.
    PhylomeDBi P56693.

    Enzyme and pathway databases

    SignaLinki P56693.

    Miscellaneous databases

    GeneWikii SOX10.
    GenomeRNAii 6663.
    NextBioi 25977.
    PROi P56693.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P56693.
    Bgeei P56693.
    CleanExi HS_SOX10.
    Genevestigatori P56693.

    Family and domain databases

    Gene3Di 1.10.30.10. 1 hit.
    InterProi IPR009071. HMG_box_dom.
    IPR022151. Sox_N.
    [Graphical view ]
    Pfami PF00505. HMG_box. 1 hit.
    PF12444. Sox_N. 1 hit.
    [Graphical view ]
    SMARTi SM00398. HMG. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47095. SSF47095. 1 hit.
    PROSITEi PS50118. HMG_BOX_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT WS4C LEU-ARG-161 INS.
    2. "The SOX10/Sox10 gene from human and mouse: sequence, expression, and transactivation by the encoded HMG domain transcription factor."
      Pusch C., Hustert E., Pfeifer D., Sudbeck P., Kist R., Roe B., Wang Z., Balling R., Blin N., Scherer G.
      Hum. Genet. 103:115-123(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "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] (ISOFORM 2).
      Tissue: Small intestine.
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. "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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    7. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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: Placenta and Skin.
    9. "Functional analysis of Sox10 mutations found in human Waardenburg-Hirschsprung patients."
      Kuhlbrodt K., Schmidt C., Sock E., Pingault V., Bondurand N., Goossens M., Wegner M.
      J. Biol. Chem. 273:23033-23038(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    10. "Sox10 is an active nucleocytoplasmic shuttle protein, and shuttling is crucial for Sox10-mediated transactivation."
      Rehberg S., Lischka P., Glaser G., Stamminger T., Wegner M., Rosorius O.
      Mol. Cell. Biol. 22:5826-5834(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOCYTOPLASMIC SHUTTLING.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "A molecular analysis of the Yemenite deaf-blind hypopigmentation syndrome: SOX10 dysfunction causes different neurocristopathies."
      Bondurand N., Kuhlbrodt K., Pingault V., Enderich J., Sajus M., Tommerup N., Warburg M., Hennekam R.C.M., Read A.P., Wegner M., Goossens M.
      Hum. Mol. Genet. 8:1785-1789(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT WS2E THR-135.
    13. "Neurological phenotype in Waardenburg syndrome type 4 correlates with novel SOX10 truncating mutations and expression in developing brain."
      Touraine R.L., Attie-Bitach T., Manceau E., Korsch E., Sarda P., Pingault V., Encha-Razavi F., Pelet A., Auge J., Nivelon-Chevallier A., Holschneider A.M., Munnes M., Doerfler W., Goossens M., Munnich A., Vekemans M., Lyonnet S.
      Am. J. Hum. Genet. 66:1496-1503(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN PCWH.
    14. "Molecular mechanism for distinct neurological phenotypes conveyed by allelic truncating mutations."
      Inoue K., Khajavi M., Ohyama T., Hirabayashi S., Wilson J., Reggin J.D., Mancias P., Butler I.J., Wilkinson M.F., Wegner M., Lupski J.R.
      Nat. Genet. 36:361-369(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN PCWH.
    15. Cited for: INVOLVEMENT IN WS2E.
    16. "A de novo missense mutation in the gene encoding the SOX10 transcription factor in a Spanish sporadic case of Waardenburg syndrome type IV."
      Morin M., Vinuela A., Rivera T., Villamar M., Moreno-Pelayo M.A., Moreno F., del Castillo I.
      Am. J. Med. Genet. A 146:1032-1037(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT WS4C VAL-157.
    17. "Aplasia of cochlear nerves and olfactory bulbs in association with SOX10 mutation."
      Barnett C.P., Mendoza-Londono R., Blaser S., Gillis J., Dupuis L., Levin A.V., Chiang P.W., Spector E., Reardon W.
      Am. J. Med. Genet. A 149:431-436(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PCWH PRO-174.
    18. "Identification and functional analysis of SOX10 missense mutations in different subtypes of Waardenburg syndrome."
      Chaoui A., Watanabe Y., Touraine R., Baral V., Goossens M., Pingault V., Bondurand N.
      Hum. Mutat. 32:1436-1449(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS WS4C TRP-106; PRO-145 AND VAL-157, VARIANTS WS2E ILE-112 AND HIS-161, VARIANTS PCWH ILE-112; HIS-131; ASN-150; PRO-174; ALA-175; LEU-175; ARG-175 AND ARG-321, CHARACTERIZATION OF VARIANTS WS4C TRP-106; PRO-145 AND VAL-157, CHARACTERIZATION OF VARIANTS WS2E ILE-112 AND HIS-161, CHARACTERIZATION OF VARIANTS PCWH HIS-131; ASN-150; PRO-174; ALA-175; LEU-175 AND ARG-175.

    Entry informationi

    Entry nameiSOX10_HUMAN
    AccessioniPrimary (citable) accession number: P56693
    Secondary accession number(s): B4DV62, Q6FHW7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: July 15, 1999
    Last modified: October 1, 2014
    This is version 147 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 22
      Human chromosome 22: 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