Full text data of OSTF1
OSTF1
[Confidence: low (only semi-automatic identification from reviews)]
Osteoclast-stimulating factor 1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Osteoclast-stimulating factor 1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q92882
ID OSTF1_HUMAN Reviewed; 214 AA.
AC Q92882; Q5W126; Q96IJ4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 30-MAY-2006, sequence version 2.
DT 22-JAN-2014, entry version 136.
DE RecName: Full=Osteoclast-stimulating factor 1;
GN Name=OSTF1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH SRC,
RP AND FUNCTION.
RC TISSUE=Bone marrow;
RX PubMed=10092216;
RX DOI=10.1002/(SICI)1097-4652(199812)177:4<636::AID-JCP14>3.3.CO;2-8;
RA Reddy S.V., Devlin R., Menaa C., Nishimura R., Choi S.J., Dallas M.,
RA Yoneda T., Roodman G.D.;
RT "Isolation and characterization of a cDNA clone encoding a novel
RT peptide (OSF) that enhances osteoclast formation and bone
RT resorption.";
RL J. Cell. Physiol. 177:636-645(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Coronary artery;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-159.
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH SMN1.
RA Roodman G.D.;
RL Unpublished observations (NOV-2000).
RN [6]
RP INTERACTION WITH SMN1.
RX PubMed=11551898; DOI=10.1074/jbc.M100233200;
RA Kurihara N., Menaa C., Maeda H., Haile D.J., Reddy S.V.;
RT "Osteoclast-stimulating factor interacts with the spinal muscular
RT atrophy gene product to stimulate osteoclast formation.";
RL J. Biol. Chem. 276:41035-41039(2001).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP INTERACTION WITH FASLG.
RX PubMed=19807924; DOI=10.1186/1471-2172-10-53;
RA Voss M., Lettau M., Janssen O.;
RT "Identification of SH3 domain interaction partners of human FasL
RT (CD178) by phage display screening.";
RL BMC Immunol. 10:53-53(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-200 AND SER-213, AND
RP MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND SER-213, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND SER-213, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP STRUCTURE BY NMR OF 15-69.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SH3 domain of human osteoclast-stimulating
RT factor 1 (OSTF1).";
RL Submitted (APR-2005) to the PDB data bank.
CC -!- FUNCTION: Induces bone resorption, acting probably through a
CC signaling cascade which results in the secretion of factor(s)
CC enhancing osteoclast formation and activity.
CC -!- SUBUNIT: Interacts with SRC and SMN1. Interacts with FASLG.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Present in osteoclasts
CC (at protein level).
CC -!- DOMAIN: The SH3 domain mediates interaction with SMN1.
CC -!- SIMILARITY: Contains 3 ANK repeats.
CC -!- SIMILARITY: Contains 1 SH3 domain.
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DR EMBL; U63717; AAB06396.1; -; mRNA.
DR EMBL; AK222596; BAD96316.1; -; mRNA.
DR EMBL; AL133548; CAH71573.1; -; Genomic_DNA.
DR EMBL; BC007459; AAH07459.1; -; mRNA.
DR RefSeq; NP_036515.4; NM_012383.4.
DR UniGene; Hs.494192; -.
DR PDB; 1X2K; NMR; -; A=15-69.
DR PDB; 1ZLM; X-ray; 1.07 A; A=12-69.
DR PDB; 3EHQ; X-ray; 2.57 A; A/B=1-214.
DR PDB; 3EHR; X-ray; 1.95 A; A/B=1-214.
DR PDBsum; 1X2K; -.
DR PDBsum; 1ZLM; -.
DR PDBsum; 3EHQ; -.
DR PDBsum; 3EHR; -.
DR ProteinModelPortal; Q92882; -.
DR SMR; Q92882; 12-193.
DR IntAct; Q92882; 8.
DR MINT; MINT-209894; -.
DR STRING; 9606.ENSP00000340836; -.
DR PhosphoSite; Q92882; -.
DR DMDM; 108885279; -.
DR PaxDb; Q92882; -.
DR PeptideAtlas; Q92882; -.
DR PRIDE; Q92882; -.
DR DNASU; 26578; -.
DR Ensembl; ENST00000346234; ENSP00000340836; ENSG00000134996.
DR GeneID; 26578; -.
DR KEGG; hsa:26578; -.
DR UCSC; uc004ajv.4; human.
DR CTD; 26578; -.
DR GeneCards; GC09P077703; -.
DR HGNC; HGNC:8510; OSTF1.
DR HPA; HPA020514; -.
DR MIM; 610180; gene.
DR neXtProt; NX_Q92882; -.
DR PharmGKB; PA32839; -.
DR eggNOG; NOG147066; -.
DR HOGENOM; HOG000286040; -.
DR HOVERGEN; HBG053379; -.
DR InParanoid; Q92882; -.
DR OMA; VELNQQN; -.
DR OrthoDB; EOG7N0C61; -.
DR EvolutionaryTrace; Q92882; -.
DR GeneWiki; OSTF1; -.
DR GenomeRNAi; 26578; -.
DR NextBio; 48926; -.
DR PRO; PR:Q92882; -.
DR Bgee; Q92882; -.
DR CleanEx; HS_OSTF1; -.
DR Genevestigator; Q92882; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005622; C:intracellular; TAS:ProtInc.
DR GO; GO:0001503; P:ossification; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR01415; ANKYRIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ANK repeat; Complete proteome; Cytoplasm;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat; SH3 domain.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 214 Osteoclast-stimulating factor 1.
FT /FTId=PRO_0000067035.
FT DOMAIN 12 71 SH3.
FT REPEAT 72 101 ANK 1.
FT REPEAT 105 135 ANK 2.
FT REPEAT 139 168 ANK 3.
FT COMPBIAS 4 11 Pro-rich.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 200 200 Phosphothreonine.
FT MOD_RES 202 202 Phosphoserine.
FT MOD_RES 213 213 Phosphoserine.
FT VARIANT 48 48 N -> S (in dbSNP:rs2295862).
FT /FTId=VAR_048309.
FT VARIANT 159 159 L -> F (in dbSNP:rs17850197).
FT /FTId=VAR_026573.
FT CONFLICT 11 11 P -> PGEG (in Ref. 4; AAH07459).
FT CONFLICT 144 145 LH -> FD (in Ref. 1; AAB06396).
FT STRAND 15 21
FT STRAND 38 43
FT STRAND 46 54
FT STRAND 57 62
FT HELIX 63 65
FT STRAND 66 68
FT STRAND 70 74
FT HELIX 76 83
FT HELIX 86 94
FT HELIX 109 115
FT HELIX 119 125
FT HELIX 143 150
FT HELIX 153 162
FT HELIX 176 179
FT HELIX 183 189
SQ SEQUENCE 214 AA; 23787 MW; 6C37F3D2B68578C3 CRC64;
MSKPPPKPVK PGQVKVFRAL YTFEPRTPDE LYFEEGDIIY ITDMSDTNWW KGTSKGRTGL
IPSNYVAEQA ESIDNPLHEA AKRGNLSWLR ECLDNRVGVN GLDKAGSTAL YWACHGGHKD
IVEMLFTQPN IELNQQNKLG DTALHAAAWK GYADIVQLLL AKGARTDLRN IEKKLAFDMA
TNAACASLLK KKQGTDAVRT LSNAEDYLDD EDSD
//
ID OSTF1_HUMAN Reviewed; 214 AA.
AC Q92882; Q5W126; Q96IJ4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 30-MAY-2006, sequence version 2.
DT 22-JAN-2014, entry version 136.
DE RecName: Full=Osteoclast-stimulating factor 1;
GN Name=OSTF1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH SRC,
RP AND FUNCTION.
RC TISSUE=Bone marrow;
RX PubMed=10092216;
RX DOI=10.1002/(SICI)1097-4652(199812)177:4<636::AID-JCP14>3.3.CO;2-8;
RA Reddy S.V., Devlin R., Menaa C., Nishimura R., Choi S.J., Dallas M.,
RA Yoneda T., Roodman G.D.;
RT "Isolation and characterization of a cDNA clone encoding a novel
RT peptide (OSF) that enhances osteoclast formation and bone
RT resorption.";
RL J. Cell. Physiol. 177:636-645(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Coronary artery;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-159.
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH SMN1.
RA Roodman G.D.;
RL Unpublished observations (NOV-2000).
RN [6]
RP INTERACTION WITH SMN1.
RX PubMed=11551898; DOI=10.1074/jbc.M100233200;
RA Kurihara N., Menaa C., Maeda H., Haile D.J., Reddy S.V.;
RT "Osteoclast-stimulating factor interacts with the spinal muscular
RT atrophy gene product to stimulate osteoclast formation.";
RL J. Biol. Chem. 276:41035-41039(2001).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP INTERACTION WITH FASLG.
RX PubMed=19807924; DOI=10.1186/1471-2172-10-53;
RA Voss M., Lettau M., Janssen O.;
RT "Identification of SH3 domain interaction partners of human FasL
RT (CD178) by phage display screening.";
RL BMC Immunol. 10:53-53(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-200 AND SER-213, AND
RP MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND SER-213, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND SER-213, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP STRUCTURE BY NMR OF 15-69.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SH3 domain of human osteoclast-stimulating
RT factor 1 (OSTF1).";
RL Submitted (APR-2005) to the PDB data bank.
CC -!- FUNCTION: Induces bone resorption, acting probably through a
CC signaling cascade which results in the secretion of factor(s)
CC enhancing osteoclast formation and activity.
CC -!- SUBUNIT: Interacts with SRC and SMN1. Interacts with FASLG.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Present in osteoclasts
CC (at protein level).
CC -!- DOMAIN: The SH3 domain mediates interaction with SMN1.
CC -!- SIMILARITY: Contains 3 ANK repeats.
CC -!- SIMILARITY: Contains 1 SH3 domain.
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DR EMBL; U63717; AAB06396.1; -; mRNA.
DR EMBL; AK222596; BAD96316.1; -; mRNA.
DR EMBL; AL133548; CAH71573.1; -; Genomic_DNA.
DR EMBL; BC007459; AAH07459.1; -; mRNA.
DR RefSeq; NP_036515.4; NM_012383.4.
DR UniGene; Hs.494192; -.
DR PDB; 1X2K; NMR; -; A=15-69.
DR PDB; 1ZLM; X-ray; 1.07 A; A=12-69.
DR PDB; 3EHQ; X-ray; 2.57 A; A/B=1-214.
DR PDB; 3EHR; X-ray; 1.95 A; A/B=1-214.
DR PDBsum; 1X2K; -.
DR PDBsum; 1ZLM; -.
DR PDBsum; 3EHQ; -.
DR PDBsum; 3EHR; -.
DR ProteinModelPortal; Q92882; -.
DR SMR; Q92882; 12-193.
DR IntAct; Q92882; 8.
DR MINT; MINT-209894; -.
DR STRING; 9606.ENSP00000340836; -.
DR PhosphoSite; Q92882; -.
DR DMDM; 108885279; -.
DR PaxDb; Q92882; -.
DR PeptideAtlas; Q92882; -.
DR PRIDE; Q92882; -.
DR DNASU; 26578; -.
DR Ensembl; ENST00000346234; ENSP00000340836; ENSG00000134996.
DR GeneID; 26578; -.
DR KEGG; hsa:26578; -.
DR UCSC; uc004ajv.4; human.
DR CTD; 26578; -.
DR GeneCards; GC09P077703; -.
DR HGNC; HGNC:8510; OSTF1.
DR HPA; HPA020514; -.
DR MIM; 610180; gene.
DR neXtProt; NX_Q92882; -.
DR PharmGKB; PA32839; -.
DR eggNOG; NOG147066; -.
DR HOGENOM; HOG000286040; -.
DR HOVERGEN; HBG053379; -.
DR InParanoid; Q92882; -.
DR OMA; VELNQQN; -.
DR OrthoDB; EOG7N0C61; -.
DR EvolutionaryTrace; Q92882; -.
DR GeneWiki; OSTF1; -.
DR GenomeRNAi; 26578; -.
DR NextBio; 48926; -.
DR PRO; PR:Q92882; -.
DR Bgee; Q92882; -.
DR CleanEx; HS_OSTF1; -.
DR Genevestigator; Q92882; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005622; C:intracellular; TAS:ProtInc.
DR GO; GO:0001503; P:ossification; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR01415; ANKYRIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ANK repeat; Complete proteome; Cytoplasm;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat; SH3 domain.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 214 Osteoclast-stimulating factor 1.
FT /FTId=PRO_0000067035.
FT DOMAIN 12 71 SH3.
FT REPEAT 72 101 ANK 1.
FT REPEAT 105 135 ANK 2.
FT REPEAT 139 168 ANK 3.
FT COMPBIAS 4 11 Pro-rich.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 200 200 Phosphothreonine.
FT MOD_RES 202 202 Phosphoserine.
FT MOD_RES 213 213 Phosphoserine.
FT VARIANT 48 48 N -> S (in dbSNP:rs2295862).
FT /FTId=VAR_048309.
FT VARIANT 159 159 L -> F (in dbSNP:rs17850197).
FT /FTId=VAR_026573.
FT CONFLICT 11 11 P -> PGEG (in Ref. 4; AAH07459).
FT CONFLICT 144 145 LH -> FD (in Ref. 1; AAB06396).
FT STRAND 15 21
FT STRAND 38 43
FT STRAND 46 54
FT STRAND 57 62
FT HELIX 63 65
FT STRAND 66 68
FT STRAND 70 74
FT HELIX 76 83
FT HELIX 86 94
FT HELIX 109 115
FT HELIX 119 125
FT HELIX 143 150
FT HELIX 153 162
FT HELIX 176 179
FT HELIX 183 189
SQ SEQUENCE 214 AA; 23787 MW; 6C37F3D2B68578C3 CRC64;
MSKPPPKPVK PGQVKVFRAL YTFEPRTPDE LYFEEGDIIY ITDMSDTNWW KGTSKGRTGL
IPSNYVAEQA ESIDNPLHEA AKRGNLSWLR ECLDNRVGVN GLDKAGSTAL YWACHGGHKD
IVEMLFTQPN IELNQQNKLG DTALHAAAWK GYADIVQLLL AKGARTDLRN IEKKLAFDMA
TNAACASLLK KKQGTDAVRT LSNAEDYLDD EDSD
//
MIM
610180
*RECORD*
*FIELD* NO
610180
*FIELD* TI
*610180 OSTEOCLAST-STIMULATING FACTOR 1; OSTF1
;;OSF;;
SH3P2
*FIELD* TX
DESCRIPTION
read more
Osteoclast-stimulating factor-1 is an intracellular protein produced by
osteoclasts that indirectly induces osteoclast formation and bone
resorption (Reddy et al., 1998).
CLONING
Using an expression cloning approach, followed by 5-prime RACE, Reddy et
al. (1998) cloned human OSTF1, which they designated OSF, from an
osteoclast-like multinucleated cell (OST-like MNC) expression library.
The deduced 214-amino acid OSTF1 protein has a predicted molecular mass
of 28 kD and shares 95% sequence identity with the mouse homolog. It
contains an N-terminal proline-rich region and a potential
N-glycosylation site, but lacks a signal sequence. OSTF1 has ankyrin
repeats and an Src homology-3 (SH3) domain that is homologous to the SH3
domain of GRB2 (108355) and FYN (137025). Northern blot analysis
detected ubiquitous expression of a 1.3-kb transcript in multiple human
tissues. In situ hybridization demonstrated OSTF1 expression in giant
cells isolated from osteosarcoma and in osteoclast-like cells in
long-term bone marrow cultures.
GENE FUNCTION
Reddy et al. (1998) demonstrated that conditioned media from HEK293
cells transfected with OSTF1 cDNA stimulated MNC formation in murine and
human bone marrow cultures. OSTF1 also increased bone resorption in the
transfected cells. Both OSTF1 activities occurred in the presence or
absence of 1,25-dihydroxy vitamin D3. Reddy et al. (1998) concluded that
OSTF1 recruits osteoclasts and activates them to resorb bone. Using
Western blot analysis of OSTF1 cellular distribution, Reddy et al.
(1998) found that OSTF1 was not secreted into the culture media. They
suggested that transient expression of OSTF1 cDNA in HEK293 cells
results in the release of other factors that enhance osteoclast
formation. In vitro affinity binding of recombinant OSTF1 with a
GST-c-Src/SH3-SH2 fusion protein suggested that the effect of OSTF1
stimulation on osteoclast formation may occur through indirect signaling
mediated by Src (190090) or other Src-related proteins.
MAPPING
By FISH, Schaub et al. (2000) mapped the OSTF1 gene to chromosome
12q24.1-q24.2. However, the International Radiation Hybrid Mapping
Consortium mapped the gene to chromosome 9 (TMAP SGC35040).
*FIELD* RF
1. Reddy, S.; Devlin, R.; Menaa, C.; Nishimura, R.; Choi, S. J.; Dallas,
M.; Yoneda, T.; Roodman, G. D.: Isolation and characterization of
a cDNA clone encoding a novel peptide (OSF) that enhances osteoclast
formation and bone resorption. J. Cell Physiol. 177: 636-645, 1998.
2. Schaub, R.; Dupont, B.; Roodman, G. D.; Leach, R. J.; Reddy, S.
V.: Assignment of OSTF1 to human chromosome bands 12q24.1-q24.2 by
in situ hybridization. Cytogenet. Cell Genet. 88: 87-88, 2000.
*FIELD* CD
Dorothy S. Reilly: 6/12/2006
*FIELD* ED
carol: 06/12/2006
*RECORD*
*FIELD* NO
610180
*FIELD* TI
*610180 OSTEOCLAST-STIMULATING FACTOR 1; OSTF1
;;OSF;;
SH3P2
*FIELD* TX
DESCRIPTION
read more
Osteoclast-stimulating factor-1 is an intracellular protein produced by
osteoclasts that indirectly induces osteoclast formation and bone
resorption (Reddy et al., 1998).
CLONING
Using an expression cloning approach, followed by 5-prime RACE, Reddy et
al. (1998) cloned human OSTF1, which they designated OSF, from an
osteoclast-like multinucleated cell (OST-like MNC) expression library.
The deduced 214-amino acid OSTF1 protein has a predicted molecular mass
of 28 kD and shares 95% sequence identity with the mouse homolog. It
contains an N-terminal proline-rich region and a potential
N-glycosylation site, but lacks a signal sequence. OSTF1 has ankyrin
repeats and an Src homology-3 (SH3) domain that is homologous to the SH3
domain of GRB2 (108355) and FYN (137025). Northern blot analysis
detected ubiquitous expression of a 1.3-kb transcript in multiple human
tissues. In situ hybridization demonstrated OSTF1 expression in giant
cells isolated from osteosarcoma and in osteoclast-like cells in
long-term bone marrow cultures.
GENE FUNCTION
Reddy et al. (1998) demonstrated that conditioned media from HEK293
cells transfected with OSTF1 cDNA stimulated MNC formation in murine and
human bone marrow cultures. OSTF1 also increased bone resorption in the
transfected cells. Both OSTF1 activities occurred in the presence or
absence of 1,25-dihydroxy vitamin D3. Reddy et al. (1998) concluded that
OSTF1 recruits osteoclasts and activates them to resorb bone. Using
Western blot analysis of OSTF1 cellular distribution, Reddy et al.
(1998) found that OSTF1 was not secreted into the culture media. They
suggested that transient expression of OSTF1 cDNA in HEK293 cells
results in the release of other factors that enhance osteoclast
formation. In vitro affinity binding of recombinant OSTF1 with a
GST-c-Src/SH3-SH2 fusion protein suggested that the effect of OSTF1
stimulation on osteoclast formation may occur through indirect signaling
mediated by Src (190090) or other Src-related proteins.
MAPPING
By FISH, Schaub et al. (2000) mapped the OSTF1 gene to chromosome
12q24.1-q24.2. However, the International Radiation Hybrid Mapping
Consortium mapped the gene to chromosome 9 (TMAP SGC35040).
*FIELD* RF
1. Reddy, S.; Devlin, R.; Menaa, C.; Nishimura, R.; Choi, S. J.; Dallas,
M.; Yoneda, T.; Roodman, G. D.: Isolation and characterization of
a cDNA clone encoding a novel peptide (OSF) that enhances osteoclast
formation and bone resorption. J. Cell Physiol. 177: 636-645, 1998.
2. Schaub, R.; Dupont, B.; Roodman, G. D.; Leach, R. J.; Reddy, S.
V.: Assignment of OSTF1 to human chromosome bands 12q24.1-q24.2 by
in situ hybridization. Cytogenet. Cell Genet. 88: 87-88, 2000.
*FIELD* CD
Dorothy S. Reilly: 6/12/2006
*FIELD* ED
carol: 06/12/2006