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Protein

Osteoclast-stimulating factor 1

Gene

Ostf1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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.By similarity

GO - Molecular functioni

  • SH3 domain binding Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Osteoclast-stimulating factor 1
Alternative name(s):
SH3 domain protein 3
Gene namesi
Name:Ostf1
Synonyms:Sh3d3, Sh3p2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:700012. Ostf1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 215214Osteoclast-stimulating factor 1PRO_0000067036Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei201 – 2011PhosphothreonineCombined sources
Modified residuei203 – 2031PhosphoserineBy similarity
Modified residuei214 – 2141PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ62422.
MaxQBiQ62422.
PaxDbiQ62422.
PRIDEiQ62422.

2D gel databases

UCD-2DPAGEQ62422.

PTM databases

iPTMnetiQ62422.
PhosphoSiteiQ62422.

Expressioni

Gene expression databases

BgeeiQ62422.
CleanExiMM_OSTF1.
GenevisibleiQ62422. MM.

Interactioni

Subunit structurei

Interacts with C-SRC and SMN1. Interacts with FASLG (By similarity).By similarity

GO - Molecular functioni

  • SH3 domain binding Source: MGI

Protein-protein interaction databases

IntActiQ62422. 1 interaction.
MINTiMINT-1869555.
STRINGi10090.ENSMUSP00000025631.

Structurei

3D structure databases

ProteinModelPortaliQ62422.
SMRiQ62422. Positions 12-193.
ModBaseiSearch...
MobiDBiSearch...

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.By similarity

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

eggNOGiENOG410IIWQ. Eukaryota.
ENOG410XR45. LUCA.
GeneTreeiENSGT00780000121977.
HOGENOMiHOG000286040.
HOVERGENiHBG053379.
InParanoidiQ62422.
OMAiVELNQQN.
OrthoDBiEOG7N0C61.
PhylomeDBiQ62422.
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.

Q62422-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKPPPKPVK PGQVKVFRAL YTFEPRTPDE LYFEEGDIIY ITDMSDTSWW
60 70 80 90 100
KGTCKGRTGL IPSNYVAEQA ESIDNPLHEA AKRGNLSWLR ECLDNRVGVN
110 120 130 140 150
GLDKAGSTAL YWACHGGHKD IVEVLFTQPN VELNQQNKLG DTALHAAAWK
160 170 180 190 200
GYADIVQLLL AKGARTDLRN NEKKLALDMA TNAACASLLK KKQQGTDGAR
210
TLSNAEDYLD DEDSD
Length:215
Mass (Da):23,783
Last modified:December 1, 2000 - v2
Checksum:iDAB682C371929B8A
GO

Sequence cautioni

The sequence AAC52641.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58888 mRNA. Translation: AAC52641.1. Different initiation.
AK002899 mRNA. Translation: BAB22442.1.
AK005525 mRNA. Translation: BAB24098.1.
AK008123 mRNA. Translation: BAB25477.1.
AK008467 mRNA. Translation: BAB25685.1.
AK010074 mRNA. Translation: BAB26683.1.
AK145949 mRNA. Translation: BAE26777.1.
AK149175 mRNA. Translation: BAE28756.1.
AK150145 mRNA. Translation: BAE29340.1.
AK155028 mRNA. Translation: BAE33000.1.
BC060986 mRNA. Translation: AAH60986.1.
CCDSiCCDS37930.1.
RefSeqiNP_059071.1. NM_017375.3.
UniGeneiMm.172222.

Genome annotation databases

EnsembliENSMUST00000025631; ENSMUSP00000025631; ENSMUSG00000024725.
GeneIDi20409.
KEGGimmu:20409.
UCSCiuc008gxs.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58888 mRNA. Translation: AAC52641.1. Different initiation.
AK002899 mRNA. Translation: BAB22442.1.
AK005525 mRNA. Translation: BAB24098.1.
AK008123 mRNA. Translation: BAB25477.1.
AK008467 mRNA. Translation: BAB25685.1.
AK010074 mRNA. Translation: BAB26683.1.
AK145949 mRNA. Translation: BAE26777.1.
AK149175 mRNA. Translation: BAE28756.1.
AK150145 mRNA. Translation: BAE29340.1.
AK155028 mRNA. Translation: BAE33000.1.
BC060986 mRNA. Translation: AAH60986.1.
CCDSiCCDS37930.1.
RefSeqiNP_059071.1. NM_017375.3.
UniGeneiMm.172222.

3D structure databases

ProteinModelPortaliQ62422.
SMRiQ62422. Positions 12-193.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ62422. 1 interaction.
MINTiMINT-1869555.
STRINGi10090.ENSMUSP00000025631.

PTM databases

iPTMnetiQ62422.
PhosphoSiteiQ62422.

2D gel databases

UCD-2DPAGEQ62422.

Proteomic databases

EPDiQ62422.
MaxQBiQ62422.
PaxDbiQ62422.
PRIDEiQ62422.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025631; ENSMUSP00000025631; ENSMUSG00000024725.
GeneIDi20409.
KEGGimmu:20409.
UCSCiuc008gxs.2. mouse.

Organism-specific databases

CTDi26578.
MGIiMGI:700012. Ostf1.

Phylogenomic databases

eggNOGiENOG410IIWQ. Eukaryota.
ENOG410XR45. LUCA.
GeneTreeiENSGT00780000121977.
HOGENOMiHOG000286040.
HOVERGENiHBG053379.
InParanoidiQ62422.
OMAiVELNQQN.
OrthoDBiEOG7N0C61.
PhylomeDBiQ62422.
TreeFamiTF314534.

Miscellaneous databases

ChiTaRSiOstf1. mouse.
NextBioi298388.
PROiQ62422.
SOURCEiSearch...

Gene expression databases

BgeeiQ62422.
CleanExiMM_OSTF1.
GenevisibleiQ62422. MM.

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. "Binding properties of SH3 peptide ligands identified from phage-displayed random peptide libraries."
    Hoffman N.G., Sparks A.B., Carter J.M., Kay B.K.
    Mol. Divers. 2:5-12(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning of ligand targets: systematic isolation of SH3 domain-containing proteins."
    Sparks A.B., Hoffman N.G., McConnell S.J., Fowlkes D.M., Kay B.K.
    Nat. Biotechnol. 14:741-744(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Embryo.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow, Kidney, Placenta, Small intestine, Sympathetic ganglion and Tongue.
  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].
    Tissue: Heart and Lung.
  5. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-201 AND SER-214, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiOSTF1_MOUSE
AccessioniPrimary (citable) accession number: Q62422
Secondary accession number(s): Q3UF05
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: March 16, 2016
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.