| General information | | DisProt: | DP00420 | | Name: | SECIS-binding protein 2 | | Synonym(s): | SEBP2_HUMAN
Selenocysteine insertion sequence-binding protein 2
SECISBP2
SBP2
| | First appeared in release: | Release 5.6 (01/10/2011) | | UniProt: | Q96T21 | | UniGene: | Hs.59804 | | SwissProt: | SEBP2_HUMAN | | TrEMBL: | | | NCBI (GI): | 52788293 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 854 | | Percent disordered: | 80% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
| | | | | |
MASEGPREPE SEGIKLSADV KPFVPRFAGL NVAWLESSEA CVFPSSAATY YPFVQEPPVT - 60
EQKIYTEDMA FGASTFPPQY LSSEITLHPY AYSPYTLDST QNVYSVPGSQ YLYNQPSCYR - 120
GFQTVKHRNE NTCPLPQEMK ALFKKKTYDE KKTYDQQKFD SERADGTISS EIKSARGSHH - 180
LSIYAENSLK SDGYHKRTDR KSRIIAKNVS TSKPEFEFTT LDFPELQGAE NNMSEIQKQP - 240
KWGPVHSVST DISLLREVVK PAAVLSKGEI VVKNNPNESV TANAATNSPS CTRELSWTPM - 300
GYVVRQTLST ELSAAPKNVT SMINLKTIAS SADPKNVSIP SSEALSSDPS YNKEKHIIHP - 360
TQKSKASQGS DLEQNEASRK NKKKKEKSTS KYEVLTVQEP PRIEDAEEFP NLAVASERRD - 420
RIETPKFQSK QQPQDNFKNN VKKSQLPVQL DLGGMLTALE KKQHSQHAKQ SSKPVVVSVG - 480
AVPVLSKECA SGERGRRMSQ MKTPHNPLDS SAPLMKKGKQ REIPKAKKPT SLKKIILKER - 540
QERKQRLQEN AVSPAFTSDD TQDGESGGDD QFPEQAELSG PEGMDELIST PSVEDKSEEP - 600
PGTELQRDTE ASHLAPNHTT FPKIHSRRFR DYCSQMLSKE VDACVTDLLK ELVRFQDRMY - 660
QKDPVKAKTK RRLVLGLREV LKHLKLKKLK CVIISPNCEK IQSKGGLDDT LHTIIDYACE - 720
QNIPFVFALN RKALGRSLNK AVPVSVVGIF SYDGAQDQFH KMVELTVAAR QAYKTMLENV - 780
QQELVGEPRP QAPPSLPTQG PSCPAEDGPP ALKEKEEPHY IEIWKKHLEA YSGCTLELEE - 840
SLEASTSQMM NLNL
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| Functional narrative |
Binds to the SECIS element in the 3'-UTR of some mRNAs encoding selenoproteins. Binding is stimulated by SELB. (UniProt).
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | | | Location: | 1 - 600 | | Length: | 600 | | Region sequence: |
MASEGPREPESEGIKLSADVKPFVPRFAGLNVAWLESSEACVFPSSAATYYPFVQEPPVT
EQKIYTEDMAFGASTFPPQYLSSEITLHPYAYSPYTLDSTQNVYSVPGSQYLYNQPSCYR
GFQTVKHRNENTCPLPQEMKALFKKKTYDEKKTYDQQKFDSERADGTISSEIKSARGSHH
LSIYAENSLKSDGYHKRTDRKSRIIAKNVSTSKPEFEFTTLDFPELQGAENNMSEIQKQP
KWGPVHSVSTDISLLREVVKPAAVLSKGEIVVKNNPNESVTANAATNSPSCTRELSWTPM
GYVVRQTLSTELSAAPKNVTSMINLKTIASSADPKNVSIPSSEALSSDPSYNKEKHIIHP
TQKSKASQGSDLEQNEASRKNKKKKEKSTSKYEVLTVQEPPRIEDAEEFPNLAVASERRD
RIETPKFQSKQQPQDNFKNNVKKSQLPVQLDLGGMLTALEKKQHSQHAKQSSKPVVVSVG
AVPVLSKECASGERGRRMSQMKTPHNPLDSSAPLMKKGKQREIPKAKKPTSLKKIILKER
QERKQRLQENAVSPAFTSDDTQDGESGGDDQFPEQAELSGPEGMDELISTPSVEDKSEEP
| | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Protein-rRNA binding
| Detection methods:
- Dynamic light scattering
- Analytical ultracentrifugation (277 K; pH: 7.8; )
- Nuclear magnetic resonance (NMR) (283 K; )
| References:
- Copeland PR, Stepanik VA, Driscoll DM. "Insight into mammalian selenocysteine insertion: domain structure and ribosome binding properties of sec insertion sequence binding protein 2." Mol Cell Biol. 2001; 21(5): 1491-8. PubMed: 11238886
- Oliéric V, Wolff P, Takeuchi A, Bec G, Birck C, Vitorino M, Kieffer B, Beniaminov A, Cavigiolio G, Theil E, Allmang C, Krol A, Dumas P. "SECIS-binding protein 2, a key player in selenoprotein synthesis, is an intrinsically disordered protein." Biochimie. 2009; 91(8): 1003-9. PubMed: 19467292
| Comments:70% of the SBP2 sequence is disordered,
whereas the RNA binding domain appears to be folded and functional. The SBP2 functional domain (amino acids 399-517) is required for full ribosome binding activity. This suggests that SBP2 may possess multiple ribosome contact sites and may remain weakly associated with the ribosome during Sec incorporation.
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| Region 2 | | Type: | Disordered | | Name: | | | Location: | 776 - 854 | | Length: | 79 | | Region sequence: |
MLENVQQELVGEPRPQAPPSLPTQGPSCPAEDGPPALKEKEEPHYIEIWKKHLEAYSGCT
LELEESLEASTSQMMNLNL | | Modification type: | Complex
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Protein-tRNA binding
| Detection methods:
| References:
- Copeland PR, Stepanik VA, Driscoll DM. "Insight into mammalian selenocysteine insertion: domain structure and ribosome binding properties of sec insertion sequence binding protein 2." Mol Cell Biol. 2001; 21(5): 1491-8. PubMed: 11238886
| Comments:
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| References |
- Copeland PR, Stepanik VA, Driscoll DM. "Insight into mammalian selenocysteine insertion: domain structure and ribosome binding properties of sec insertion sequence binding protein 2." Mol Cell Biol. 2001; 21(5): 1491-8. PubMed: 11238886
- Olieric V, Wolff P, Takeuchi A, Bec G, Birck C, Vitorino M, Kieffer B, Beniaminov A, Cavigiolio G, Theil E, Allmang C, Krol A, Dumas P. "SECIS-binding protein 2, a key player in selenoprotein synthesis, is an intrinsically disordered protein." Biochimie. 2009; 91(8): 1003-9. PubMed: 19467292
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| Comments |
Sent for AV 1-12-2011 (PubMed: 11238886)
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