Primary Information |
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| BoMiProt ID | Bomi5177 |
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| Protein Name | DNA endonuclease RBBP8/CtBP-interacting protein/Retinoblastoma-binding protein 8/Retinoblastoma-interacting protein and myosin-like/Sporulation in the absence of SPO11 protein 2 homolog |
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| Organism | Bos taurus |
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| Uniprot ID | A6QNQ6 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_001095436.1 |
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| Aminoacid Length | 757 |
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| Molecular Weight | 85265 |
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| FASTA Sequence |
Download |
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| Gene Name | RBBP8/CTIP |
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| Gene ID | 512977 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | DNA binding activity; identical protein binding activity; and single-stranded DNA endodeoxyribonuclease activity.Acts upstream of or within G1/S transition of mitotic cell cycle and blastocyst hatching. Predicted to be located in nucleoplasm. |
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| PTMs | phosphorylation,Ubl conjugation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|A6QNQ6|CTIP_BOVIN DNA endonuclease RBBP8 OS=Bos taurus OX=9913 GN=RBBP8 PE=2 SV=2
MNLSGSSCGSPSSADVSNDFKDLWTKLKEYHDKETQGLQVKVTKLKKERILDAQRLEEFF
TKNQQLREQQKVLHETIKVLEDRLRAGLCDRCAVTEEHMRKKQQEFENIRQQNLKLITEL
MNEKNTLQEENKKLSEQLQQKIENDQPHKATDLESEEDVIPDSPITTFSFSGTNRLRRKE
NLRVRYIEQTHAKLEHSGCAHELRTVPKSSAHPQHKPKESEILVADTCDQSQAPVAKPHG
KSSYTPDNLATVVAETLGLCVQEESESRGPQS*272PLGDELYHCLEGDHKKQAFEECRRNSED
NLRFSDSKT*309PFQEELTTRVS*320S*321PVFGAPSNVKSSLGLNTSLSPS*343LLETGKKTHLKTVPLSNTSAPGPEKPRSKSEDGTLITHHHLGTEVNKIPSQSSSNKQMLINKNTSEPISEQGNIGHS
KDTDRDKHVVPLKSLGGRTKRKKIEEESEDEVICPQASFDKENAFPFPLDSHSSMNGDYV
MDKPLDLSDRFSAIQRQEKSQGCENSKIRFRQVTLYEALKPIPRDSSSSRKALSGSCGLT
KDSPEEPCLQESLFQSLSKSPDNKTLLQIKEENPVFKIPLRPRESFETENLFDDTKGAGS
HEPIKIKTRSVRGACEVASVLQLNPCRIAKTKSLQNNQDVSFENIQWSIDPGADLS*656QYKM
GVTVDDTKDGSQSRLAGETVDMDCTLVSETMLLKLKKQEQKGEESPNGERKMNDS*715LEDMF
DRTTHEEYESCLAESFPQVADEEKELSTTTKKPNISW
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| Predicted Disorder Regions | 5-13, 134-154, 204-210, 272-288, 425-436, 526-541, 649-651, 711-756 |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Significance of PTMs | Phosphorylation by CDK1 is essential for the recruitment to DNA and the DNA repair function. Phosphorylated on Ser-321 as cells enter G2 phase. Phosphorylation at Thr-309, probably catalyzed by CDK2, is required for PIN1-binding, while phosphorylation at Ser-272 serves as a PIN1 isomerization site. Phosphorylation at Thr-309 is cell-cycle dependent. It steadily increases during S phase, peaks at late S/G2 phase, and drops at G1.Ubiquitinated through 'Lys-48' by the E3 CUL3-KLHL15 complex; this modification leads to proteasomal degradation. |
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