Q92882 (OSTF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Osteoclast-stimulating factor 1

Gene names

Name:

OSTF1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	214 AA.
Sequence status	Complete.
Protein existence	Evidence 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.11
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 component	Cytoplasm
Coding sequence diversity	Polymorphism
Domain	ANK repeat Repeat SH3 domain
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ossification Traceable author statement Ref.1. Source: ProtInc signal transduction Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell intracellular Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 214

214

Osteoclast-stimulating factor 1

PRO_0000067035

Regions

Domain

12 – 71

60

SH3

Repeat

72 – 101

30

ANK 1

Repeat

105 – 135

31

ANK 2

Repeat

139 – 168

30

ANK 3

Compositional bias

4 – 11

8

Pro-rich

Amino acid modifications

Modified residue

200

1

Phosphothreonine Ref.12

Modified residue

202

1

Phosphoserine Ref.13 Ref.15

Modified residue

213

1

Phosphoserine Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.15

Natural variations

Natural variant

48

1

N → S.
Corresponds to variant rs2295862 [ dbSNP | Ensembl ].

VAR_048309

Natural variant

159

1

L → F. Ref.4
Corresponds to variant rs17850197 [ dbSNP | Ensembl ].

VAR_026573

Experimental info

Sequence conflict

11

1

P → PGEG in AAH07459. Ref.4

Sequence conflict

144 – 145

2

LH → FD in AAB06396. Ref.1

Secondary structure

1

.

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214

Helix Strand Turn

Details...

Beta strand

15 – 21

7

Beta strand

38 – 43

6

Beta strand

46 – 54

9

Beta strand

57 – 62

6

Helix

63 – 65

3

Beta strand

66 – 68

3

Beta strand

70 – 74

5

Helix

76 – 83

8

Helix

86 – 94

9

Helix

109 – 115

7

Helix

119 – 125

7

Helix

143 – 150

8

Helix

153 – 162

10

Helix

176 – 179

4

Helix

183 – 189

7

Sequences

	Sequence		Length	Mass (Da)
	Q92882 [UniParc]. Last modified May 30, 2006. Version 2. Checksum: 6C37F3D2B68578C3	FASTA	214	23,787
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Liver.
[11]	"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.
[12]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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].
[15]	"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, MASS SPECTROMETRY.
[16]	"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.

IPI

IPI00414836.

RefSeq

NP_036515.4. NM_012383.4.

UniGene

Hs.494192.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1X2K	NMR	-	A	15-69	[»]
1ZLM	X-ray	1.07	A	12-69	[»]
3EHQ	X-ray	2.57	A/B	1-214	[»]
3EHR	X-ray	1.95	A/B	1-214	[»]

ProteinModelPortal

Q92882.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q92882. 3 interactions.

MINT

MINT-209894.

STRING

9606.ENSP00000340836.

PTM databases

PhosphoSite

Q92882.

Polymorphism databases

DMDM

108885279.

Proteomic databases

PaxDb

Q92882.

PeptideAtlas

Q92882.

PRIDE

Q92882.

Protocols and materials databases

DNASU

26578.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000346234; ENSP00000340836; ENSG00000134996.

GeneID

26578.

KEGG

hsa:26578.

UCSC

uc004ajv.4. human.

Organism-specific databases

CTD

26578.

GeneCards

GC09P077703.

HGNC

HGNC:8510. OSTF1.

HPA

HPA020514.

MIM

610180. gene.

neXtProt

NX_Q92882.

PharmGKB

PA32839.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG147066.

HOGENOM

HOG000286040.

HOVERGEN

HBG053379.

InParanoid

Q92882.

OMA

HGGHKDV.

OrthoDB

EOG4Z62PH.

Gene expression databases

Bgee

Q92882.

CleanEx

HS_OSTF1.

Genevestigator

Q92882.

GermOnline

ENSG00000134996. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.20. 1 hit.

InterPro

IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR000108. p67phox.
IPR001452. SH3_domain.
[Graphical view]

Pfam

PF12796. Ank_2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR01415. ANKYRIN.
PR00499. P67PHOX.
PR00452. SH3DOMAIN.

SMART

SM00248. ANK. 3 hits.
SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF48403. ANK. 1 hit.
SSF50044. SH3. 1 hit.

PROSITE

PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q92882.

GenomeRNAi

26578.

NextBio

48926.

SOURCE

Search...

Entry information

Entry name

OSTF1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 132 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.