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Q8VI67

- SP7_MOUSE

UniProt

Q8VI67 - SP7_MOUSE

Protein

Transcription factor Sp7

Gene

Sp7

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    Functioni

    Transcriptional activator essential for osteoblast differentiation. Binds to SP1 and EKLF consensus sequences and to other G/C-rich sequences.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri291 – 31525C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri321 – 34525C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri351 – 37323C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DEAD/H-box RNA helicase binding Source: BHF-UCL
    2. DNA binding Source: MGI
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. hematopoietic stem cell differentiation Source: Ensembl
    2. osteoblast differentiation Source: MGI
    3. positive regulation of stem cell differentiation Source: Ensembl
    4. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    5. regulation of transcription from RNA polymerase II promoter Source: MGI
    6. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription factor Sp7
    Alternative name(s):
    C22
    Zinc finger protein osterix
    Gene namesi
    Name:Sp7
    Synonyms:Osx
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:2153568. Sp7.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. nucleus Source: MGI

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Death in the immediate postnatal period due to difficulty in breathing. Mice rapidly become cyanotic and die within 15 min of birth. New-born homozygous show severe inward bending of forelimbs and hindlimbs. They develop a normal cartilage skeleton but fail to form bone and to express osteoblast-specific marker genes. In endochondral skeletal elements, mesenchymal cells together with osteoclasts and blood vessels, invade the mineralized cartilage matrix.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 428428Transcription factor Sp7PRO_0000047151Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki55 – 55Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki227 – 227Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

    Post-translational modificationi

    Ubiquitination at leads to proteasomal degradation. SP7 is a short-live protein with an endogenous half-life of approximately 12 hours By similarity.By similarity

    Keywords - PTMi

    Isopeptide bond, Ubl conjugation

    Proteomic databases

    PRIDEiQ8VI67.

    PTM databases

    PhosphoSiteiQ8VI67.

    Expressioni

    Tissue specificityi

    Osteoblast/chondrocyte specific.

    Gene expression databases

    BgeeiQ8VI67.
    CleanExiMM_SP7.
    GenevestigatoriQ8VI67.

    Interactioni

    Subunit structurei

    Interacts with NO66; the interaction is direct and inhibits transcription activator activity.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NO66Q9H6W36EBI-7608836,EBI-2513645From a different organism.
    No66Q9JJF33EBI-7608836,EBI-7608809

    Protein-protein interaction databases

    BioGridi228354. 6 interactions.
    DIPiDIP-46090N.
    IntActiQ8VI67. 4 interactions.
    MINTiMINT-7709305.
    STRINGi10090.ENSMUSP00000077596.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8VI67.
    SMRiQ8VI67. Positions 287-373.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Contains 3 C2H2-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri291 – 31525C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri321 – 34525C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri351 – 37323C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5048.
    GeneTreeiENSGT00750000117314.
    HOGENOMiHOG000231067.
    HOVERGENiHBG036899.
    InParanoidiQ8VI67.
    KOiK09197.
    OMAiPKTMGDA.
    OrthoDBiEOG73FQMR.
    PhylomeDBiQ8VI67.
    TreeFamiTF350150.

    Family and domain databases

    Gene3Di3.30.160.60. 3 hits.
    InterProiIPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view]
    SMARTiSM00355. ZnF_C2H2. 3 hits.
    [Graphical view]
    PROSITEiPS00028. ZINC_FINGER_C2H2_1. 3 hits.
    PS50157. ZINC_FINGER_C2H2_2. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8VI67-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASSLLEEEA HYGSSPLAML TAACSKFGGS SPLRDSTTLG KGGTKKPYAD    50
    LSAPKTMGDA YPAPFSSTNG LLSPAGSPPA PASGYANDYP PFPHSFPGPT 100
    GAQDPGLLVP KGHSSSDCLP SVYTSLDMTH PYGSWYKAGI HAGISPGPGN 150
    TPTPWWDMHP GGNWLGGGQG QGDGLQGTLS TGPAQPPLNP QLPTYPSDFA 200
    PLNPAPYPAP HLLQPGPQHV LPQDVYKPKA VGNSGQLEGS GAAKPPRGAG 250
    TGGSGGYAGS GAGRSTCDCP NCQELERLGA AAAGLRKKPI HSCHIPGCGK 300
    VYGKASHLKA HLRWHTGERP FVCNWLFCGK RFTRSDELER HVRTHTREKK 350
    FTCLLCSKRF TRSDHLSKHQ RTHGEPGPGP PPSGPKELGE GRSVGEEEAN 400
    QPPRSSTSPA PPEKAHGGSP EQSNLLEI 428
    Length:428
    Mass (Da):44,718
    Last modified:March 1, 2002 - v1
    Checksum:iB794988958743586
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti64 – 641P → L in BAC36263. (PubMed:16141072)Curated
    Sequence conflicti130 – 1301H → Y in BAC36774. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF184902 mRNA. Translation: AAL60067.1.
    AK032521 mRNA. Translation: BAC27908.1.
    AK076229 mRNA. Translation: BAC36263.1.
    AK077375 mRNA. Translation: BAC36774.1.
    CCDSiCCDS37228.1.
    RefSeqiNP_569725.1. NM_130458.3.
    XP_006520582.1. XM_006520519.1.
    UniGeneiMm.263284.

    Genome annotation databases

    EnsembliENSMUST00000078508; ENSMUSP00000077596; ENSMUSG00000060284.
    GeneIDi170574.
    KEGGimmu:170574.
    UCSCiuc007xvm.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF184902 mRNA. Translation: AAL60067.1 .
    AK032521 mRNA. Translation: BAC27908.1 .
    AK076229 mRNA. Translation: BAC36263.1 .
    AK077375 mRNA. Translation: BAC36774.1 .
    CCDSi CCDS37228.1.
    RefSeqi NP_569725.1. NM_130458.3.
    XP_006520582.1. XM_006520519.1.
    UniGenei Mm.263284.

    3D structure databases

    ProteinModelPortali Q8VI67.
    SMRi Q8VI67. Positions 287-373.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 228354. 6 interactions.
    DIPi DIP-46090N.
    IntActi Q8VI67. 4 interactions.
    MINTi MINT-7709305.
    STRINGi 10090.ENSMUSP00000077596.

    PTM databases

    PhosphoSitei Q8VI67.

    Proteomic databases

    PRIDEi Q8VI67.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000078508 ; ENSMUSP00000077596 ; ENSMUSG00000060284 .
    GeneIDi 170574.
    KEGGi mmu:170574.
    UCSCi uc007xvm.1. mouse.

    Organism-specific databases

    CTDi 121340.
    MGIi MGI:2153568. Sp7.

    Phylogenomic databases

    eggNOGi COG5048.
    GeneTreei ENSGT00750000117314.
    HOGENOMi HOG000231067.
    HOVERGENi HBG036899.
    InParanoidi Q8VI67.
    KOi K09197.
    OMAi PKTMGDA.
    OrthoDBi EOG73FQMR.
    PhylomeDBi Q8VI67.
    TreeFami TF350150.

    Miscellaneous databases

    NextBioi 370123.
    PROi Q8VI67.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8VI67.
    CleanExi MM_SP7.
    Genevestigatori Q8VI67.

    Family and domain databases

    Gene3Di 3.30.160.60. 3 hits.
    InterProi IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view ]
    SMARTi SM00355. ZnF_C2H2. 3 hits.
    [Graphical view ]
    PROSITEi PS00028. ZINC_FINGER_C2H2_1. 3 hits.
    PS50157. ZINC_FINGER_C2H2_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The novel zinc finger-containing transcription factor osterix is required for osteoblast differentiation and bone formation."
      Nakashima K., Zhou X., Kunkel G., Zhang Z., Deng J.M., Behringer R.R., de Crombrugghe B.
      Cell 108:17-29(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Head and Olfactory neuron.
    3. "Regulation of the osteoblast-specific transcription factor Osterix by NO66, a Jumonji family histone demethylase."
      Sinha K.M., Yasuda H., Coombes M.M., Dent S.Y., de Crombrugghe B.
      EMBO J. 29:68-79(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NO66.

    Entry informationi

    Entry nameiSP7_MOUSE
    AccessioniPrimary (citable) accession number: Q8VI67
    Secondary accession number(s): Q8C5R3, Q8C6A7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 16, 2003
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 98 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3