Primary Information |
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| BoMiProt ID | Bomi8127 |
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| Protein Name | Poly(U)-binding-splicing factor PUF60/60 kDa poly(U)-binding-splicing factor |
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| Organism | Bos taurus |
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| Uniprot ID | Q2HJG2 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_001039598.1 |
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| Aminoacid Length | 530 |
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| Molecular Weight | 57087 |
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| FASTA Sequence |
Download |
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| Gene Name | PUF60 |
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| Gene ID | 512824 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | encodes a splicing factor that interacts directly with SF3B4 and plays a role in the recognition of the 3-prime splice site during splicing and recruitment of U2 snRNP and subsequently U5 snRNP to the intron for splicing. |
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| Biochemical Properties | The C-terminal domain of PUF60, the PUMP domain, is distantly related to the RNA-recognition motif domain, and is probably important in protein–protein interactions.PUF60 forms SDSresistant dimers with an apparent molecular weight of 130 kDa, explaining the aberrant mobility of this protein
on SDS-polyacrylamide gels. |
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| PTMs | Acetylation on Lys, Phosphorylation on Thr and Ser, Ubl conjugation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q2HJG2|PUF60_BOVIN Poly(U)-binding-splicing factor PUF60 OS=Bos taurus OX=9913 GN=PUF60 PE=2 SV=1
MATATIALGTDSIKMENGQGTAAKLGLPPLT*41PEQQEALQKAKKYAMEQSIKSVLVKQTIA
HQQQQLTNLQMAAVTMGFGDPLS*83PLQSMAAQRQRALAIMCRVYVGSIYYELGEDTIRQAF
APFGPIKSIDMSWDSVTMKHKGFAFVEYEVPEAAQLALEQMNSVMLGGRNIKVGRPSNIG
QAQPIIDQLAEEARAFNRIYVASVHQDLSDDDIKS*215VFEAFGKIKSCTLARDPTTGKHKGY
GFIEYEKAQSSQDAVSSMNLFDLGGQYLRVGKAVTPPMPLLTPAT*285PGGLPPAAAVAAAAA
TAKITAQEAVAGAAVLGTLATPGLVSPALTLAQPLGALPQAVMAAQAPGVITGVTPARPP
IPVTIPSVGVVNPILASPPTLGLLEPKKEKEEEELFPESERPEMLSEQEHMSISGSSARH
MVMQKLLRKQESTVMVLRNMVDPKDIDDDLEGEVTEECGKFGAVNRVIIYQEKQGEEEDA
EIIVKIFVEFSVASETHKAIQDLNGRWFAGRKVVAEVYDQERFDNSDLSA
|
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Bibliography | PAGE-McCAW, P., AMONLIRDVIMAN, K., & SHARP, P. (1999). PUF60: A novel U2AF65-related splicing activity. RNA, 5(12), 1548-1560. doi:10.1017/S1355838299991938 |
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