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Q92882 (OSTF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Osteoclast-stimulating factor 1
Gene names
Name:OSTF1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length214 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Interacts with SRC and SMN1. Interacts with FASLG. Ref.1 Ref.5 Ref.6 Ref.12

Subcellular location

Cytoplasm Probable.

Tissue specificity

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

Domain

The SH3 domain mediates interaction with SMN1.

Sequence similarities

Contains 3 ANK repeats.

Contains 1 SH3 domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   DomainANK repeat
Repeat
SH3 domain
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processossification

Traceable author statement Ref.1. Source: ProtInc

signal transduction

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

intracellular

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 17500595PubMed 23275563. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HTTP428585EBI-1051152,EBI-466029

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.17
Chain2 – 214213Osteoclast-stimulating factor 1
PRO_0000067035

Regions

Domain12 – 7160SH3
Repeat72 – 10130ANK 1
Repeat105 – 13531ANK 2
Repeat139 – 16830ANK 3
Compositional bias4 – 118Pro-rich

Amino acid modifications

Modified residue21N-acetylserine Ref.17
Modified residue2001Phosphothreonine Ref.13
Modified residue2021Phosphoserine Ref.14 Ref.16
Modified residue2131Phosphoserine Ref.7 Ref.8 Ref.9 Ref.10 Ref.13 Ref.14 Ref.16

Natural variations

Natural variant481N → S.
Corresponds to variant rs2295862 [ dbSNP | Ensembl ].
VAR_048309
Natural variant1591L → F. Ref.4
Corresponds to variant rs17850197 [ dbSNP | Ensembl ].
VAR_026573

Experimental info

Sequence conflict111P → PGEG in AAH07459. Ref.4
Sequence conflict144 – 1452LH → FD in AAB06396. Ref.1

Secondary structure

............................. 214
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q92882 [UniParc].

Last modified May 30, 2006. Version 2.
Checksum: 6C37F3D2B68578C3

FASTA21423,787
        10         20         30         40         50         60 
MSKPPPKPVK PGQVKVFRAL YTFEPRTPDE LYFEEGDIIY ITDMSDTNWW KGTSKGRTGL 

        70         80         90        100        110        120 
IPSNYVAEQA ESIDNPLHEA AKRGNLSWLR ECLDNRVGVN GLDKAGSTAL YWACHGGHKD 

       130        140        150        160        170        180 
IVEMLFTQPN IELNQQNKLG DTALHAAAWK GYADIVQLLL AKGARTDLRN IEKKLAFDMA 

       190        200        210 
TNAACASLLK KKQGTDAVRT LSNAEDYLDD EDSD 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U63717 mRNA. Translation: AAB06396.1.
AK222596 mRNA. Translation: BAD96316.1.
AL133548 Genomic DNA. Translation: CAH71573.1.
BC007459 mRNA. Translation: AAH07459.1.
CCDSCCDS6651.1.
RefSeqNP_036515.4. NM_012383.4.
UniGeneHs.494192.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1X2KNMR-A15-69[»]
1ZLMX-ray1.07A12-69[»]
3EHQX-ray2.57A/B1-214[»]
3EHRX-ray1.95A/B1-214[»]
ProteinModelPortalQ92882.
SMRQ92882. Positions 12-193.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117747. 19 interactions.
IntActQ92882. 7 interactions.
MINTMINT-209894.
STRING9606.ENSP00000340836.

PTM databases

PhosphoSiteQ92882.

Polymorphism databases

DMDM108885279.

Proteomic databases

MaxQBQ92882.
PaxDbQ92882.
PeptideAtlasQ92882.
PRIDEQ92882.

Protocols and materials databases

DNASU26578.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000346234; ENSP00000340836; ENSG00000134996.
GeneID26578.
KEGGhsa:26578.
UCSCuc004ajv.4. human.

Organism-specific databases

CTD26578.
GeneCardsGC09P077703.
HGNCHGNC:8510. OSTF1.
HPAHPA020514.
MIM610180. gene.
neXtProtNX_Q92882.
PharmGKBPA32839.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG147066.
HOGENOMHOG000286040.
HOVERGENHBG053379.
InParanoidQ92882.
OMAVELNQQN.
OrthoDBEOG7N0C61.
PhylomeDBQ92882.
TreeFamTF314534.

Gene expression databases

BgeeQ92882.
CleanExHS_OSTF1.
GenevestigatorQ92882.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamPF12796. Ank_2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR01415. ANKYRIN.
PR00452. SH3DOMAIN.
SMARTSM00248. ANK. 3 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ92882.
GeneWikiOSTF1.
GenomeRNAi26578.
NextBio48926.
PROQ92882.
SOURCESearch...

Entry information

Entry nameOSTF1_HUMAN
AccessionPrimary (citable) accession number: Q92882
Secondary accession number(s): Q5W126, Q96IJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 30, 2006
Last modified: July 9, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM