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Protein

Osteoclast-stimulating factor 1

Gene

OSTF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 - 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 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:8510. OSTF1.

Subcellular locationi

  1. Cytoplasm Curated

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA32839.

Polymorphism and mutation databases

BioMutaiOSTF1.
DMDMi108885279.

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 – 2131Phosphoserine8 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
EFSO432813EBI-1051152,EBI-718488
HTTP428585EBI-1051152,EBI-466029
RELQ048643EBI-1051152,EBI-307352
SDCBPO005603EBI-1051152,EBI-727004
TRIM54Q9BYV23EBI-1051152,EBI-2130429

Protein-protein interaction databases

BioGridi117747. 25 interactions.
IntActiQ92882. 11 interactions.
MINTiMINT-209894.
STRINGi9606.ENSP00000340836.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00780000121977.
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

        10         20         30         40         50
MSKPPPKPVK PGQVKVFRAL YTFEPRTPDE LYFEEGDIIY ITDMSDTNWW
60 70 80 90 100
KGTSKGRTGL IPSNYVAEQA ESIDNPLHEA AKRGNLSWLR ECLDNRVGVN
110 120 130 140 150
GLDKAGSTAL YWACHGGHKD IVEMLFTQPN IELNQQNKLG DTALHAAAWK
160 170 180 190 200
GYADIVQLLL AKGARTDLRN IEKKLAFDMA TNAACASLLK KKQGTDAVRT
210
LSNAEDYLDD EDSD
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:
EMBLi
GenBanki
DDBJi
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 and mutation databases

BioMutaiOSTF1.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi117747. 25 interactions.
IntActiQ92882. 11 interactions.
MINTiMINT-209894.
STRINGi9606.ENSP00000340836.

PTM databases

PhosphoSiteiQ92882.

Polymorphism and mutation databases

BioMutaiOSTF1.
DMDMi108885279.

Proteomic databases

MaxQBiQ92882.
PaxDbiQ92882.
PeptideAtlasiQ92882.
PRIDEiQ92882.

Protocols and materials databases

DNASUi26578.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi26578.
GeneCardsiGC09P077703.
HGNCiHGNC:8510. OSTF1.
HPAiHPA020514.
MIMi610180. gene.
neXtProtiNX_Q92882.
PharmGKBiPA32839.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG147066.
GeneTreeiENSGT00780000121977.
HOGENOMiHOG000286040.
HOVERGENiHBG053379.
InParanoidiQ92882.
OMAiVELNQQN.
OrthoDBiEOG7N0C61.
PhylomeDBiQ92882.
TreeFamiTF314534.

Miscellaneous databases

ChiTaRSiOSTF1. human.
EvolutionaryTraceiQ92882.
GeneWikiiOSTF1.
GenomeRNAii26578.
NextBioi48926.
PROiQ92882.
SOURCEiSearch...

Gene expression databases

BgeeiQ92882.
CleanExiHS_OSTF1.
GenevestigatoriQ92882.

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]
ProtoNetiSearch...

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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "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: April 29, 2015
This is version 150 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.