Search by BoMiProt ID - Bomi5177


Primary Information

BoMiProt ID Bomi5177
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
Organism Bos taurus
Uniprot IDA6QNQ6
Milk FractionWhey
Ref Sequence ID NP_001095436.1
Aminoacid Length 757
Molecular Weight 85265
FASTA Sequence Download
Gene Name RBBP8/CTIP
Gene ID 512977
Protein Existence Status reviewed

Secondary Information

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.
PTMs phosphorylation,Ubl conjugation
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
Predicted Disorder Regions 5-13, 134-154, 204-210, 272-288, 425-436, 526-541, 649-651, 711-756
DisProt Annotation
TM Helix Prediction No TM helices
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.