CTIP_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CTIP_MOUSE
• UniProt AC: Q80YR6
• Protein Name: DNA endonuclease RBBP8
• Gene Name: Rbbp8
• Organism: Mus musculus (Mouse).
• Sequence Length: 893
• Subcellular Localization: Nucleus . Chromosome . Associates with sites of DNA damage in S/G2 phase. Ubiquitinated RBBP8 binds to chromatin following DNA damage.
• Protein Description: Endonuclease that cooperates with the MRE11-RAD50-NBN (MRN) complex in DNA-end resection, the first step of double-strand break (DSB) repair through the homologous recombination (HR) pathway. HR is restricted to S and G2 phases of the cell cycle and preferentially repairs DSBs resulting from replication fork collapse. Key determinant of DSB repair pathway choice, as it commits cells to HR by preventing classical non-homologous end-joining (NHEJ). Functions downstream of the MRN complex and ATM, promotes ATR activation and its recruitment to DSBs in the S/G2 phase facilitating the generation of ssDNA. Component of the BRCA1-RBBP8 complex that regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage. During immunoglobulin heavy chain class-switch recombination, promotes microhomology-mediated alternative end joining (A-NHEJ) and plays an essential role in chromosomal translocations..
• Protein Sequence: MSISGSGCGSPNSADASNDFKELWTKLKEYHDKEVQGLQVKVTKLKKERILDAQRLEEFFTKNQQLRDQQKVLQETIKILEDRLRAGLCDRCAVTEEHMHKKQQEFENIRQQNLKLITELMNEKNTLQEENKKLSEQLQQKMENGQQDQVAELACEENIIPDSPVTSFSFSGINRLRKKENLHVRYVEQTHTKLERSLCTNELRKISKDSAPAPVNSEEHEILVADTCDQNHSPLSKICETSSYPTDKTSFNLDTVVAETLGLNGQEESEPQGPMSPLGSELYHCLKEDHKKHPFMESARSKEDSLRFSDSASKTPPQEFTTRASSPVFGATSTVKAHLGLNTSFSPSLLDIGKKNLLKTAPFSNIAVSRSEKVRSKSEDNALFTQHSLGSEVKVISQSFSSKQILTNKTVSDSVDEQCSADHMNTTVADKYLVPLKSLGGKASKRKRTEEESEHAVKCPQACFDKENALPFPMENQFSMNGDHVMDKPLDLSDRFAATQRQEKNHGNETSKNKLKQATIYEALKPIPKGSSSGRKALSGDCMPAKDSWETYCLQPRSLQSSSKFSPDQKTPLQIKEENPVFKTPPCSQESLETENLFGDVKGTGSLVPTKVKSRAVHGGCELASVLQLNPCRVAKTKALPSNQDTSFENIQWSVDPGADLSQYKMDVTVIDTKDSSHSRLGGETVDMDCTLVSETVLLKMKKQEQKERSPNGDIKMNDSLEDMFDRTTHEEYESCLADSFSQVPDEEELPDTTKKTNIPADKQDGVKQKAFVGPYFKDKERETSIQNFPHIEVVRKKEERRKLLGHTCKECEIYYADLPAEEREKKLASCSRHRFRYIPPNTPENFWEVGFPSTQTCLERGYIKEDLDLSPRPKRRQPYNAVFSPKGKEQRT

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSISGSGCG ------CCCCCCCCC		25619855
4	Phosphorylation	----MSISGSGCGSP ----CCCCCCCCCCC		25619855
6	Phosphorylation	--MSISGSGCGSPNS --CCCCCCCCCCCCC		25619855
10	Phosphorylation	ISGSGCGSPNSADAS CCCCCCCCCCCCCCC		25619855
13	Phosphorylation	SGCGSPNSADASNDF CCCCCCCCCCCCHHH		25619855
17	Phosphorylation	SPNSADASNDFKELW CCCCCCCCHHHHHHH		25619855
210	Phosphorylation	LRKISKDSAPAPVNS HHHHCCCCCCCCCCC		25777480
217	Phosphorylation	SAPAPVNSEEHEILV CCCCCCCCCCCEEEE		25777480
227	Phosphorylation	HEILVADTCDQNHSP CEEEEEECCCCCCCC		25266776
233	Phosphorylation	DTCDQNHSPLSKICE ECCCCCCCCHHHHHC		25266776
236	Phosphorylation	DQNHSPLSKICETSS CCCCCCHHHHHCCCC		25293948
276	Phosphorylation	SEPQGPMSPLGSELY CCCCCCCCCCHHHHH		-
309	Phosphorylation	KEDSLRFSDSASKTP HHHHCCCCCCCCCCC		28066266
311	Phosphorylation	DSLRFSDSASKTPPQ HHCCCCCCCCCCCCH		25619855
313	Phosphorylation	LRFSDSASKTPPQEF CCCCCCCCCCCCHHH		25619855
314	Acetylation	RFSDSASKTPPQEFT CCCCCCCCCCCHHHC		30985583
315	Phosphorylation	FSDSASKTPPQEFTT CCCCCCCCCCHHHCC		25619855
321	Phosphorylation	KTPPQEFTTRASSPV CCCCHHHCCCCCCCC		28066266
322	Phosphorylation	TPPQEFTTRASSPVF CCCHHHCCCCCCCCC		28066266
325	Phosphorylation	QEFTTRASSPVFGAT HHHCCCCCCCCCCCC		23375375
326	Phosphorylation	EFTTRASSPVFGATS HHCCCCCCCCCCCCC		26824392
332	Phosphorylation	SSPVFGATSTVKAHL CCCCCCCCCCEEHHH		25619855
333	Phosphorylation	SPVFGATSTVKAHLG CCCCCCCCCEEHHHC		25619855
343	Phosphorylation	KAHLGLNTSFSPSLL EHHHCCCCCCCHHHH		26643407
344	Phosphorylation	AHLGLNTSFSPSLLD HHHCCCCCCCHHHHH		26745281
346	Phosphorylation	LGLNTSFSPSLLDIG HCCCCCCCHHHHHHC		26643407
348	Phosphorylation	LNTSFSPSLLDIGKK CCCCCCHHHHHHCCC		26643407
376	Phosphorylation	SRSEKVRSKSEDNAL CCCHHHCCCCCCCCC		25266776
378	Phosphorylation	SEKVRSKSEDNALFT CHHHCCCCCCCCCCC		25266776
431	Acetylation	MNTTVADKYLVPLKS CCCCHHHHHHEEHHH		-
525	Acetylation	ATIYEALKPIPKGSS HHHHHHHCCCCCCCC		-
561	Phosphorylation	LQPRSLQSSSKFSPD CCCCCCCCCCCCCCC		25777480
563	Phosphorylation	PRSLQSSSKFSPDQK CCCCCCCCCCCCCCC		25777480
566	Phosphorylation	LQSSSKFSPDQKTPL CCCCCCCCCCCCCCC		28507225
584	Phosphorylation	EENPVFKTPPCSQES CCCCCCCCCCCCHHH		26643407
588	Phosphorylation	VFKTPPCSQESLETE CCCCCCCCHHHHHHC		25266776
591	Phosphorylation	TPPCSQESLETENLF CCCCCHHHHHHCCCC		25266776
594	Phosphorylation	CSQESLETENLFGDV CCHHHHHHCCCCCCC		26643407
602	Acetylation	ENLFGDVKGTGSLVP CCCCCCCCCCCCCCC		-
662	Phosphorylation	VDPGADLSQYKMDVT ECCCCCHHHCEEEEE		-
677	Phosphorylation	VIDTKDSSHSRLGGE EEECCCCCCCCCCCE		-
710	Phosphorylation	KQEQKERSPNGDIKM HHHHHHCCCCCCCCC		23375375
720	Phosphorylation	GDIKMNDSLEDMFDR CCCCCCHHHHHHHCC		21149613
742	Phosphorylation	SCLADSFSQVPDEEE HHHHHCCCCCCCHHH		-
757	Phosphorylation	LPDTTKKTNIPADKQ CCCCCCCCCCCCCCC		28973931
843	Phosphorylation	FRYIPPNTPENFWEV CCCCCCCCCCCCCCC		-
871	Phosphorylation	IKEDLDLSPRPKRRQ CCCCCCCCCCCCCCC		26824392
885	Phosphorylation	QPYNAVFSPKGKEQR CCCCCCCCCCCCCCC		25266776

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
662	S	Phosphorylation	Kinase	ATM	Q62388	Uniprot
742	S	Phosphorylation	Kinase	ATM	Q62388	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
48	K	ubiquitylation	Ubiquitinated through 'Lys-48' by the E3 CUL3-KLHL15 complex; this modification leads to proteasomal degradation.	-
276	S	Phosphorylation	Phosphorylation at Thr-315 is required for PIN1-binding, while phosphorylation at Ser-276 serves as a PIN1 isomerization site.	-
315	T	Phosphorylation	Phosphorylation at Thr-315 is cell-cycle dependent.	-
315	T	Phosphorylation	Phosphorylation at Thr-315 is required for PIN1-binding, while phosphorylation at Ser-276 serves as a PIN1 isomerization site.	-
326	S	Phosphorylation	Phosphorylated at Ser-326 as cells enter G2 phase.	-
843	T	Phosphorylation	Phosphorylation at Thr-843 by CDK1 is essential for the recruitment to DNA and the DNA repair function.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of CTIP_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of CTIP_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.