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Protein

Follistatin-related protein 3

Gene

FSTL3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Isoform 1 or the secreted form is a binding and antagonizing protein for members of the TGF-beta family, such us activin, BMP2 and MSTN. Inhibits activin A-, activin B-, BMP2- and MSDT-induced cellular signaling; more effective on activin A than on activin B. Involved in bone formation; inhibits osteoclast differentiationc. Involved in hematopoiesis; involved in differentiation of hemopoietic progenitor cells, increases hematopoietic cell adhesion to fibronectin and seems to contribute to the adhesion of hematopoietic precursor cells to the bone marrow stroma. Isoform 2 or the nuclear form is probably involved in transcriptional regulation via interaction with MLLT10.6 Publications

GO - Molecular functioni

  • activin binding Source: UniProtKB
  • fibronectin binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Osteogenesis, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-HSA-2473224. Antagonism of Activin by Follistatin.
SIGNORiO95633.

Protein family/group databases

MEROPSiI01.968.

Names & Taxonomyi

Protein namesi
Recommended name:
Follistatin-related protein 3
Alternative name(s):
Follistatin-like protein 3
Follistatin-related gene protein
Gene namesi
Name:FSTL3
Synonyms:FLRG
ORF Names:UNQ674/PRO1308
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:3973. FSTL3.

Subcellular locationi

Isoform 2 :
  • Nucleus

  • Note: Although alternative initiation has been demonstrated and resulted in different localization, the major source of nuclear FSTL3 appears not to depend on translation initiation at Met-27 according to.1 Publication

GO - Cellular componenti

  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • Golgi apparatus Source: Ensembl
  • neuron projection terminus Source: Ensembl
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • secretory granule Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Secreted

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving FSTL3 is found in a case of B-cell chronic lymphocytic leukemia. Translocation t(11;19)(q13;p13) with CCDN1.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi27 – 271M → A: Nuclear localization. 1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA28390.

Polymorphism and mutation databases

BioMutaiFSTL3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26261 PublicationAdd
BLAST
Chaini27 – 263237Follistatin-related protein 3PRO_0000010115Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi38 ↔ 61PROSITE-ProRule annotation
Disulfide bondi48 ↔ 92PROSITE-ProRule annotation
Disulfide bondi62 ↔ 95PROSITE-ProRule annotation
Glycosylationi73 – 731N-linked (GlcNAc...)1 Publication
Disulfide bondi99 ↔ 110
Disulfide bondi104 ↔ 119
Disulfide bondi121 ↔ 153
Disulfide bondi125 ↔ 146
Disulfide bondi135 ↔ 167
Disulfide bondi171 ↔ 182
Disulfide bondi176 ↔ 192
Disulfide bondi195 ↔ 229
Disulfide bondi200 ↔ 222
Disulfide bondi211 ↔ 243
Glycosylationi215 – 2151N-linked (GlcNAc...)1 Publication
Modified residuei255 – 2551Phosphoserine; by FAM20C1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiO95633.
PaxDbiO95633.
PeptideAtlasiO95633.
PRIDEiO95633.
TopDownProteomicsiO95633-1. [O95633-1]

PTM databases

iPTMnetiO95633.

Miscellaneous databases

PMAP-CutDBO95633.

Expressioni

Tissue specificityi

Expressed in a wide range of tissues.1 Publication

Gene expression databases

BgeeiO95633.
CleanExiHS_FSTL3.
ExpressionAtlasiO95633. baseline and differential.
GenevisibleiO95633. HS.

Organism-specific databases

HPAiCAB024899.
HPA045378.

Interactioni

Subunit structurei

Interacts with INHBA and INHBB. Interacts with FN1. Interacts with ADAM12. Isoform 2 interacts with MLLT10; the interaction enhances MLLT10 in vitro transcriptional activity and self-association. Interacts with MSTN.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ADAM12O43184-24EBI-2625790,EBI-2625865

GO - Molecular functioni

  • activin binding Source: UniProtKB
  • fibronectin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi115562. 1 interaction.
IntActiO95633. 2 interactions.
STRINGi9606.ENSP00000166139.

Structurei

Secondary structure

1
263
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi37 – 404Combined sources
Beta strandi50 – 556Combined sources
Helixi58 – 625Combined sources
Beta strandi67 – 726Combined sources
Helixi81 – 866Combined sources
Beta strandi93 – 953Combined sources
Beta strandi97 – 993Combined sources
Beta strandi108 – 1114Combined sources
Beta strandi113 – 1164Combined sources
Beta strandi118 – 1214Combined sources
Beta strandi126 – 1283Combined sources
Beta strandi134 – 1363Combined sources
Beta strandi141 – 1444Combined sources
Helixi145 – 1539Combined sources
Beta strandi161 – 1666Combined sources
Beta strandi169 – 1713Combined sources
Beta strandi181 – 1844Combined sources
Beta strandi190 – 1934Combined sources
Beta strandi204 – 2074Combined sources
Beta strandi210 – 2123Combined sources
Beta strandi217 – 2204Combined sources
Helixi221 – 23111Combined sources
Beta strandi237 – 2415Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KCXNMR-A97-169[»]
3B4VX-ray2.48C/D/G/H27-263[»]
3SEKX-ray2.40C36-244[»]
ProteinModelPortaliO95633.
SMRiO95633. Positions 32-244.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO95633.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 10772TBPROSITE-ProRule annotationAdd
BLAST
Domaini99 – 11921Follistatin-like 1Add
BLAST
Domaini113 – 16957Kazal-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini170 – 19324Follistatin-like 2Add
BLAST
Domaini189 – 24557Kazal-like 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 follistatin-like domains.Curated
Contains 2 Kazal-like domains.PROSITE-ProRule annotation
Contains 1 TB (TGF-beta binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG3649. Eukaryota.
ENOG410YC3T. LUCA.
GeneTreeiENSGT00440000033501.
HOGENOMiHOG000261649.
HOVERGENiHBG051666.
InParanoidiO95633.
OMAiLPCKDSC.
OrthoDBiEOG7GBFXR.
PhylomeDBiO95633.
TreeFamiTF106409.

Family and domain databases

Gene3Di3.90.290.10. 1 hit.
InterProiIPR003645. Fol_N.
IPR015369. Follistatin/Osteonectin_EGF.
IPR002350. Kazal_dom.
IPR017878. TB_dom.
[Graphical view]
PfamiPF09289. FOLN. 1 hit.
PF07648. Kazal_2. 2 hits.
[Graphical view]
SMARTiSM00274. FOLN. 2 hits.
SM00280. KAZAL. 2 hits.
[Graphical view]
SUPFAMiSSF57581. SSF57581. 1 hit.
PROSITEiPS51465. KAZAL_2. 2 hits.
PS51364. TB. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform 1 (identifier: O95633-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRPGAPGPLW PLPWGALAWA VGFVSSMGSG NPAPGGVCWL QQGQEATCSL
60 70 80 90 100
VLQTDVTRAE CCASGNIDTA WSNLTHPGNK INLLGFLGLV HCLPCKDSCD
110 120 130 140 150
GVECGPGKAC RMLGGRPRCE CAPDCSGLPA RLQVCGSDGA TYRDECELRA
160 170 180 190 200
ARCRGHPDLS VMYRGRCRKS CEHVVCPRPQ SCVVDQTGSA HCVVCRAAPC
210 220 230 240 250
PVPSSPGQEL CGNNNVTYIS SCHMRQATCF LGRSIGVRHA GSCAGTPEEP
260
PGGESAEEEE NFV
Length:263
Mass (Da):27,663
Last modified:May 1, 1999 - v1
Checksum:i6A9AB86ADD4FD09C
GO
Isoform 2 (identifier: O95633-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: Missing.

Show »
Length:237
Mass (Da):24,960
Checksum:i499A1E50592DDFE4
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2626Missing in isoform 2. CuratedVSP_038553Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U76702 mRNA. Translation: AAC64321.1.
AY358917 mRNA. Translation: AAQ89276.1.
AK291958 mRNA. Translation: BAF84647.1.
CH471242 Genomic DNA. Translation: EAW61165.1.
BC005839 mRNA. Translation: AAH05839.1.
CCDSiCCDS12040.1. [O95633-1]
RefSeqiNP_005851.1. NM_005860.2. [O95633-1]
UniGeneiHs.529038.

Genome annotation databases

EnsembliENST00000166139; ENSP00000166139; ENSG00000070404. [O95633-1]
GeneIDi10272.
KEGGihsa:10272.
UCSCiuc002lpk.2. human. [O95633-1]

Keywords - Coding sequence diversityi

Alternative initiation, Chromosomal rearrangement

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U76702 mRNA. Translation: AAC64321.1.
AY358917 mRNA. Translation: AAQ89276.1.
AK291958 mRNA. Translation: BAF84647.1.
CH471242 Genomic DNA. Translation: EAW61165.1.
BC005839 mRNA. Translation: AAH05839.1.
CCDSiCCDS12040.1. [O95633-1]
RefSeqiNP_005851.1. NM_005860.2. [O95633-1]
UniGeneiHs.529038.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KCXNMR-A97-169[»]
3B4VX-ray2.48C/D/G/H27-263[»]
3SEKX-ray2.40C36-244[»]
ProteinModelPortaliO95633.
SMRiO95633. Positions 32-244.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115562. 1 interaction.
IntActiO95633. 2 interactions.
STRINGi9606.ENSP00000166139.

Protein family/group databases

MEROPSiI01.968.

PTM databases

iPTMnetiO95633.

Polymorphism and mutation databases

BioMutaiFSTL3.

Proteomic databases

MaxQBiO95633.
PaxDbiO95633.
PeptideAtlasiO95633.
PRIDEiO95633.
TopDownProteomicsiO95633-1. [O95633-1]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000166139; ENSP00000166139; ENSG00000070404. [O95633-1]
GeneIDi10272.
KEGGihsa:10272.
UCSCiuc002lpk.2. human. [O95633-1]

Organism-specific databases

CTDi10272.
GeneCardsiFSTL3.
HGNCiHGNC:3973. FSTL3.
HPAiCAB024899.
HPA045378.
MIMi605343. gene.
neXtProtiNX_O95633.
PharmGKBiPA28390.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3649. Eukaryota.
ENOG410YC3T. LUCA.
GeneTreeiENSGT00440000033501.
HOGENOMiHOG000261649.
HOVERGENiHBG051666.
InParanoidiO95633.
OMAiLPCKDSC.
OrthoDBiEOG7GBFXR.
PhylomeDBiO95633.
TreeFamiTF106409.

Enzyme and pathway databases

ReactomeiR-HSA-2473224. Antagonism of Activin by Follistatin.
SIGNORiO95633.

Miscellaneous databases

ChiTaRSiFSTL3. human.
EvolutionaryTraceiO95633.
GeneWikiiFSTL3.
GenomeRNAii10272.
PMAP-CutDBO95633.
PROiO95633.
SOURCEiSearch...

Gene expression databases

BgeeiO95633.
CleanExiHS_FSTL3.
ExpressionAtlasiO95633. baseline and differential.
GenevisibleiO95633. HS.

Family and domain databases

Gene3Di3.90.290.10. 1 hit.
InterProiIPR003645. Fol_N.
IPR015369. Follistatin/Osteonectin_EGF.
IPR002350. Kazal_dom.
IPR017878. TB_dom.
[Graphical view]
PfamiPF09289. FOLN. 1 hit.
PF07648. Kazal_2. 2 hits.
[Graphical view]
SMARTiSM00274. FOLN. 2 hits.
SM00280. KAZAL. 2 hits.
[Graphical view]
SUPFAMiSSF57581. SSF57581. 1 hit.
PROSITEiPS51465. KAZAL_2. 2 hits.
PS51364. TB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "FLRG (follistatin-related gene), a new target of chromosomal rearrangement in malignant blood disorders."
    Hayette S., Gadoux M., Martel S., Bertrand S., Tigaud I., Magaud J.-P., Rimokh R.
    Oncogene 16:2949-2954(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHROMOSOMAL TRANSLOCATION.
    Tissue: Placenta.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Placenta.
  6. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-41.
  7. "Human follistatin-related protein: a structural homologue of follistatin with nuclear localization."
    Tortoriello D.V., Sidis Y., Holtzman D.A., Holmes W.E., Schneyer A.L.
    Endocrinology 142:3426-3434(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  8. "Transcription activation of FLRG and follistatin by activin A, through Smad proteins, participates in a negative feedback loop to modulate activin A function."
    Bartholin L., Maguer-Satta V., Hayette S., Martel S., Gadoux M., Corbo L., Magaud J.P., Rimokh R.
    Oncogene 21:2227-2235(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Differential binding and neutralization of activins A and B by follistatin and follistatin like-3 (FSTL-3/FSRP/FLRG)."
    Schneyer A., Schoen A., Quigg A., Sidis Y.
    Endocrinology 144:1671-1674(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INHBA AND INHBB.
  10. "Follistatin-related gene (FLRG) expression in human endometrium: sex steroid hormones regulate the expression of FLRG in cultured human endometrial stromal cells."
    Wang H.Q., Takebayashi K., Tsuchida K., Nishimura M., Noda Y.
    J. Clin. Endocrinol. Metab. 88:4432-4439(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. "FLRG, member of the follistatin family, a new player in hematopoiesis."
    Maguer-Satta V., Rimokh R.
    Mol. Cell. Endocrinol. 225:109-118(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HEMATOPOIESIS.
  12. "FLRG, a new ADAM12-associated protein, modulates osteoclast differentiation."
    Bartholin L., Destaing O., Forissier S., Martel S., Maguer-Satta V., Jurdic P., Rimokh R.
    Biol. Cell 97:577-588(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN OSTEOCLAST DIFFERENTIATION, INTERACTION WITH ADAM8 AND ADAM12.
  13. "Differential biosynthesis and intracellular transport of follistatin isoforms and follistatin-like-3."
    Saito S., Sidis Y., Mukherjee A., Xia Y., Schneyer A.
    Endocrinology 146:5052-5062(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ALTERNATIVE INITIATION, MUTAGENESIS OF MET-27.
  14. "A novel role for fibronectin type I domain in the regulation of human hematopoietic cell adhesiveness through binding to follistatin domains of FLRG and follistatin."
    Maguer-Satta V., Forissier S., Bartholin L., Martel S., Jeanpierre S., Bachelard E., Rimokh R.
    Exp. Cell Res. 312:434-442(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HEMATOPOIESIS, INTERACTION WITH FN1.
  15. "AF10-dependent transcription is enhanced by its interaction with FLRG."
    Forissier S., Razanajaona D., Ay A.S., Martel S., Bartholin L., Rimokh R.
    Biol. Cell 99:563-571(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRANSCRIPTION REGULATION, INTERACTION WITH MLLT10.
  16. "Characterization of follistatin-related gene as a negative regulatory factor for activin family members during mouse heart development."
    Takehara-Kasamatsu Y., Tsuchida K., Nakatani M., Murakami T., Kurisaki A., Hashimoto O., Ohuchi H., Kurose H., Mori K., Kagami S., Noji S., Sugino H.
    J. Med. Invest. 54:276-288(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MSTN.
  17. Cited for: PHOSPHORYLATION AT SER-255.
  18. "The structure of FSTL3.activin A complex. Differential binding of N-terminal domains influences follistatin-type antagonist specificity."
    Stamler R., Keutmann H.T., Sidis Y., Kattamuri C., Schneyer A., Thompson T.B.
    J. Biol. Chem. 283:32831-32838(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 27-263 IN COMPLEX WITH INHBA, DISULFIDE BONDS, GLYCOSYLATION AT ASN-215.
  19. "Structure of myostatin.follistatin-like 3: N-terminal domains of follistatin-type molecules exhibit alternate modes of binding."
    Cash J.N., Angerman E.B., Kattamuri C., Nolan K., Zhao H., Sidis Y., Keutmann H.T., Thompson T.B.
    J. Biol. Chem. 287:1043-1053(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 36-244 IN COMPLEX WITH MOUSE GDF8, GLYCOSYLATION AT ASN-73, DISULFIDE BONDS.

Entry informationi

Entry nameiFSTL3_HUMAN
AccessioniPrimary (citable) accession number: O95633
Secondary accession number(s): A8K7E3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: May 1, 1999
Last modified: June 8, 2016
This is version 143 of the entry and version 1 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.