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Q92882

- OSTF1_HUMAN

UniProt

Q92882 - OSTF1_HUMAN

Protein

Osteoclast-stimulating factor 1

Gene

OSTF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (30 May 2006)
      Previous versions | rss
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    Functioni

    Induces bone resorption, acting probably through a signaling cascade which results in the secretion of factor(s) enhancing osteoclast formation and activity.1 Publication

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. ossification Source: ProtInc
    2. signal transduction Source: ProtInc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Osteoclast-stimulating factor 1
    Gene namesi
    Name:OSTF1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:8510. OSTF1.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt
    3. intracellular Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA32839.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 214213Osteoclast-stimulating factor 1PRO_0000067035Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei200 – 2001Phosphothreonine1 Publication
    Modified residuei202 – 2021Phosphoserine2 Publications
    Modified residuei213 – 2131Phosphoserine7 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ92882.
    PaxDbiQ92882.
    PeptideAtlasiQ92882.
    PRIDEiQ92882.

    PTM databases

    PhosphoSiteiQ92882.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Present in osteoclasts (at protein level).1 Publication

    Gene expression databases

    BgeeiQ92882.
    CleanExiHS_OSTF1.
    GenevestigatoriQ92882.

    Organism-specific databases

    HPAiHPA020514.

    Interactioni

    Subunit structurei

    Interacts with SRC and SMN1. Interacts with FASLG.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HTTP428585EBI-1051152,EBI-466029

    Protein-protein interaction databases

    BioGridi117747. 19 interactions.
    IntActiQ92882. 7 interactions.
    MINTiMINT-209894.
    STRINGi9606.ENSP00000340836.

    Structurei

    Secondary structure

    1
    214
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi15 – 217
    Beta strandi38 – 436
    Beta strandi46 – 549
    Beta strandi57 – 626
    Helixi63 – 653
    Beta strandi66 – 683
    Beta strandi70 – 745
    Helixi76 – 838
    Helixi86 – 949
    Helixi109 – 1157
    Helixi119 – 1257
    Helixi143 – 1508
    Helixi153 – 16210
    Helixi176 – 1794
    Helixi183 – 1897

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1X2KNMR-A15-69[»]
    1ZLMX-ray1.07A12-69[»]
    3EHQX-ray2.57A/B1-214[»]
    3EHRX-ray1.95A/B1-214[»]
    ProteinModelPortaliQ92882.
    SMRiQ92882. Positions 12-193.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92882.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini12 – 7160SH3PROSITE-ProRule annotationAdd
    BLAST
    Repeati72 – 10130ANK 1Add
    BLAST
    Repeati105 – 13531ANK 2Add
    BLAST
    Repeati139 – 16830ANK 3Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi4 – 118Pro-rich

    Domaini

    The SH3 domain mediates interaction with SMN1.

    Sequence similaritiesi

    Contains 3 ANK repeats.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Repeat, SH3 domain

    Phylogenomic databases

    eggNOGiNOG147066.
    HOGENOMiHOG000286040.
    HOVERGENiHBG053379.
    InParanoidiQ92882.
    OMAiVELNQQN.
    OrthoDBiEOG7N0C61.
    PhylomeDBiQ92882.
    TreeFamiTF314534.

    Family and domain databases

    Gene3Di1.25.40.20. 1 hit.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF12796. Ank_2. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    PRINTSiPR01415. ANKYRIN.
    PR00452. SH3DOMAIN.
    SMARTiSM00248. ANK. 3 hits.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    SSF50044. SSF50044. 1 hit.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q92882-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKPPPKPVK PGQVKVFRAL YTFEPRTPDE LYFEEGDIIY ITDMSDTNWW    50
    KGTSKGRTGL IPSNYVAEQA ESIDNPLHEA AKRGNLSWLR ECLDNRVGVN 100
    GLDKAGSTAL YWACHGGHKD IVEMLFTQPN IELNQQNKLG DTALHAAAWK 150
    GYADIVQLLL AKGARTDLRN IEKKLAFDMA TNAACASLLK KKQGTDAVRT 200
    LSNAEDYLDD EDSD 214
    Length:214
    Mass (Da):23,787
    Last modified:May 30, 2006 - v2
    Checksum:i6C37F3D2B68578C3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 111P → PGEG in AAH07459. (PubMed:15489334)Curated
    Sequence conflicti144 – 1452LH → FD in AAB06396. (PubMed:10092216)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti48 – 481N → S.
    Corresponds to variant rs2295862 [ dbSNP | Ensembl ].
    VAR_048309
    Natural varianti159 – 1591L → F.1 Publication
    Corresponds to variant rs17850197 [ dbSNP | Ensembl ].
    VAR_026573

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U63717 mRNA. Translation: AAB06396.1.
    AK222596 mRNA. Translation: BAD96316.1.
    AL133548 Genomic DNA. Translation: CAH71573.1.
    BC007459 mRNA. Translation: AAH07459.1.
    CCDSiCCDS6651.1.
    RefSeqiNP_036515.4. NM_012383.4.
    UniGeneiHs.494192.

    Genome annotation databases

    EnsembliENST00000346234; ENSP00000340836; ENSG00000134996.
    GeneIDi26578.
    KEGGihsa:26578.
    UCSCiuc004ajv.4. human.

    Polymorphism databases

    DMDMi108885279.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U63717 mRNA. Translation: AAB06396.1 .
    AK222596 mRNA. Translation: BAD96316.1 .
    AL133548 Genomic DNA. Translation: CAH71573.1 .
    BC007459 mRNA. Translation: AAH07459.1 .
    CCDSi CCDS6651.1.
    RefSeqi NP_036515.4. NM_012383.4.
    UniGenei Hs.494192.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1X2K NMR - A 15-69 [» ]
    1ZLM X-ray 1.07 A 12-69 [» ]
    3EHQ X-ray 2.57 A/B 1-214 [» ]
    3EHR X-ray 1.95 A/B 1-214 [» ]
    ProteinModelPortali Q92882.
    SMRi Q92882. Positions 12-193.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117747. 19 interactions.
    IntActi Q92882. 7 interactions.
    MINTi MINT-209894.
    STRINGi 9606.ENSP00000340836.

    PTM databases

    PhosphoSitei Q92882.

    Polymorphism databases

    DMDMi 108885279.

    Proteomic databases

    MaxQBi Q92882.
    PaxDbi Q92882.
    PeptideAtlasi Q92882.
    PRIDEi Q92882.

    Protocols and materials databases

    DNASUi 26578.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000346234 ; ENSP00000340836 ; ENSG00000134996 .
    GeneIDi 26578.
    KEGGi hsa:26578.
    UCSCi uc004ajv.4. human.

    Organism-specific databases

    CTDi 26578.
    GeneCardsi GC09P077703.
    HGNCi HGNC:8510. OSTF1.
    HPAi HPA020514.
    MIMi 610180. gene.
    neXtProti NX_Q92882.
    PharmGKBi PA32839.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG147066.
    HOGENOMi HOG000286040.
    HOVERGENi HBG053379.
    InParanoidi Q92882.
    OMAi VELNQQN.
    OrthoDBi EOG7N0C61.
    PhylomeDBi Q92882.
    TreeFami TF314534.

    Miscellaneous databases

    EvolutionaryTracei Q92882.
    GeneWikii OSTF1.
    GenomeRNAii 26578.
    NextBioi 48926.
    PROi Q92882.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q92882.
    CleanExi HS_OSTF1.
    Genevestigatori Q92882.

    Family and domain databases

    Gene3Di 1.25.40.20. 1 hit.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF12796. Ank_2. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PRINTSi PR01415. ANKYRIN.
    PR00452. SH3DOMAIN.
    SMARTi SM00248. ANK. 3 hits.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    SSF50044. SSF50044. 1 hit.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of a cDNA clone encoding a novel peptide (OSF) that enhances osteoclast formation and bone resorption."
      Reddy S.V., Devlin R., Menaa C., Nishimura R., Choi S.J., Dallas M., Yoneda T., Roodman G.D.
      J. Cell. Physiol. 177:636-645(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH SRC, FUNCTION.
      Tissue: Bone marrow.
    2. 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].
      Tissue: Coronary artery.
    3. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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], VARIANT PHE-159.
      Tissue: Kidney.
    5. Roodman G.D.
      Unpublished observations (NOV-2000)
      Cited for: INTERACTION WITH SMN1.
    6. "Osteoclast-stimulating factor interacts with the spinal muscular atrophy gene product to stimulate osteoclast formation."
      Kurihara N., Menaa C., Maeda H., Haile D.J., Reddy S.V.
      J. Biol. Chem. 276:41035-41039(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SMN1.
    7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
      Voss M., Lettau M., Janssen O.
      BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FASLG.
    13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-200 AND SER-213, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND SER-213, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND SER-213, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    18. "Solution structure of the SH3 domain of human osteoclast-stimulating factor 1 (OSTF1)."
      RIKEN structural genomics initiative (RSGI)
      Submitted (APR-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 15-69.

    Entry informationi

    Entry nameiOSTF1_HUMAN
    AccessioniPrimary (citable) accession number: Q92882
    Secondary accession number(s): Q5W126, Q96IJ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 30, 2006
    Last modified: October 1, 2014
    This is version 144 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3