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Q92882

- OSTF1_HUMAN

UniProt

Q92882 - OSTF1_HUMAN

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Protein
Osteoclast-stimulating factor 1
Gene
OSTF1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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 Inferred

GO - Cellular componenti

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

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 1
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiQ92882.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 7160SH3
Add
BLAST
Repeati72 – 10130ANK 1
Add
BLAST
Repeati105 – 13531ANK 2
Add
BLAST
Repeati139 – 16830ANK 3
Add
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.
Contains 1 SH3 domain.

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111P → PGEG in AAH07459. 1 Publication
Sequence conflicti144 – 1452LH → FD in AAB06396. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 143 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

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