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Reviewed, UniProtKB/Swiss-Prot Q92882 (OSTF1_HUMAN)

Last modified February 9, 2010. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

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

Protein attributes

Sequence length214 AA.
Sequence statusComplete.
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. Ref.1 Ref.5 Ref.6

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
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processossification Ref.1

Traceable author statement. Source: ProtInc

signal transduction Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionidentical protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 214214Osteoclast-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 residue2001Phosphothreonine Ref.11 Ref.13 Ref.14
Modified residue2021Phosphoserine Ref.13 Ref.8 Ref.9 Ref.10
Modified residue2131Phosphoserine Ref.11 Ref.13 Ref.14 Ref.8 Ref.9 Ref.10 Ref.7

Natural variations

Natural variant481N → S: dbSNP rs2295862.
VAR_048309
Natural variant1591L → F: dbSNP rs17850197. Ref.4
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
Q92882-1 [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: 10092216] [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: 15164053] [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: 15489334] [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: 11551898] [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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, MASS SPECTROMETRY.
Tissue: Epithelium.
[8]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND SER-213, MASS SPECTROMETRY.
[9]"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: 18088087] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND SER-213, MASS SPECTROMETRY.
Tissue: Platelet.
[10]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND SER-213, MASS SPECTROMETRY.
[11]"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: 18318008] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-200 AND SER-213, MASS SPECTROMETRY.
Tissue: Liver.
[12]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[13]"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: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-200; SER-202 AND SER-213, MASS SPECTROMETRY.
[14]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-200 AND SER-213, MASS SPECTROMETRY.
Tissue: T-cell.
[15]"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.
IPIIPI00414836.
RefSeqNP_036515.4.
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[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ92882. 6 interactions.
STRINGQ92882.

PTM databases

PhosphoSiteQ92882.

Proteomic databases

PeptideAtlasQ92882.
PRIDEQ92882.

Genome annotation databases

EnsemblENST00000346234; ENSP00000340836; ENSG00000134996; Homo sapiens. [Genome view]
GeneID26578.
KEGGhsa:26578.
UCSCuc004ajv.2. human.

Organism-specific databases

CTD26578.
GeneCardsGC09P076893.
H-InvDBHIX0008106.
HGNCHGNC:8510. OSTF1.
MIM610180. gene.
PharmGKBPA32839.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG14459.
HOGENOMHBG377860.
HOVERGENQ92882.
InParanoidQ92882.
OMAVELNQQN.
OrthoDBEOG9V19KG.

Gene expression databases

ArrayExpressQ92882.
BgeeQ92882.
CleanExHS_OSTF1.
GenevestigatorQ92882.
GermOnlineENSG00000134996. Homo sapiens.

Family and domain databases

InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR000108. Neu_cyt_fact_2.
IPR001452. SH3_domain.
IPR020473. SH3_region.
[Graphical view]
Gene3DG3DSA:1.25.40.20. ANK. 1 hit.
PfamPF00023. Ank. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00499. P67PHOX.
PR00452. SH3DOMAIN.
SMARTSM00248. ANK. 3 hits.
SM00326. SH3. 1 hit.
[Graphical view]
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio48926.
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: February 9, 2010
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 9

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents