INT3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: INT3_MOUSE
• UniProt AC: Q7TPD0
• Protein Name: Integrator complex subunit 3
• Gene Name: Ints3
• Organism: Mus musculus (Mouse).
• Sequence Length: 1041
• Subcellular Localization: Nucleus . Cytoplasm . Localizes to nuclear foci following DNA damage.
• Protein Description: Component of the Integrator (INT) complex. The Integrator complex is involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes. Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex.; Component of the SOSS complex, a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint. The SOSS complex associates with single-stranded DNA at DNA lesions and influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair and maintenance of genomic stability. The SOSS complex is required for efficient homologous recombination-dependent repair of double-strand breaks (DSBs) and ATM-dependent signaling pathways. In the SOSS complex, it is required for the assembly of the complex and for stabilization of the complex at DNA damage sites..
• Protein Sequence: MELQKGKGTVAAAASGAAGGGGGGAGAGAPGGGRLLLSTSLDAKDELEERLERCMSIVTSMTAGVSEREANDALNAYVCKGPPQHEEICLGLFTLVLTEPAQAQKCYRDLALVSRDGMNIVLNKINQLLMEKYLKLQDTCRTQLVWLVRELVKSGVLGADGVCMTFMKQIAGGDVTAKNIWLAESVLDILTEQREWVLKSSILIAMAVYTYLRLIVDHHGTAQLQTLRQKEVDFCISLLRERFMECLMIGRDLVRLLQNVARIPEFELLWKDIIHNPQALSPQFTGILQLLQSRTSRKFLACRLTPDMETKLLFMTSRVRFGQQKRYQDWFQRQYLSTPDSQSLRCDLIRYICGVVHPSNEVLSSDILPRWAIIGWLLTTCTSNVAASNAKLALFYDWLFFSPEKDSIMNIEPAILVMHHSMKPHPAITATLLDFMCRIIPNFYPPLEGHVRQGVFSSLNHIVEKRVLAHLAPLFDNPKLDKELRSMLREKFPEFCSSPSPPVEVKIEEPVSMEMDNHLSDKDESCYDNAEAAFSDDEEDLNSKGKKREFRFHPIKETVVEEPVDVTPYLDQLDESLRDKVLQLQKGSDTEAQCEVMQEIVDQVLEEDFDSEQLSVLASCLQELFKAHFRGEVLPEEVTEESLEESVGKPLYLIFRNLCQMQEDNSSFSLLLDLLSELYQKQPKIGYHLLYYLRASKAAAGKMNLYESFAQATQLGDLHTCLMMDMKACQEDDVRLLCHLTPSIYTEFPDETLRSGELLNMIVAVIDSAQLQELVCHVMMGNLVMFRKDSVLNILIQSLDWETFEQYCAWQLFLAHNIPLETIIPILQHLKYKEHPEALSCLLLQLRREKPSEEMVKMVLSRPCHPDDQFTTSILRHWCMKHDELLAEHIKALLIKNNSLPRKRQSLRSSSSKLAQLTLEQILEHLDNLRLNLANTKQNFFSQTPILQALQHVQASCDEAHKMKFSDLFSLAEEYEDSSTKPPKSRRKAALSSPRSRKNATQPPNAEEESGSSSASEEEDTKPKPTKRKRKGSSAVGSDSD

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
1	Acetylation	-------MELQKGKG -------CCCCCCCC	47.93	-
9	Phosphorylation	ELQKGKGTVAAAASG CCCCCCCHHHHHHCC	15.51	22817900
15	Phosphorylation	GTVAAAASGAAGGGG CHHHHHHCCCCCCCC	25.00	22817900
38	Phosphorylation	GGGRLLLSTSLDAKD CCCCEEEECCCCCHH	18.87	28285833
107	Phosphorylation	PAQAQKCYRDLALVS HHHHHHHHHHHHHHC	17.75	24899341
346	S-nitrosylation	PDSQSLRCDLIRYIC CCHHHHHHHHHHHHH	6.39	21278135
346	S-nitrosocysteine	PDSQSLRCDLIRYIC CCHHHHHHHHHHHHH	6.39	-
479	Ubiquitination	APLFDNPKLDKELRS HHHCCCHHHHHHHHH	75.47	22790023
486	Phosphorylation	KLDKELRSMLREKFP HHHHHHHHHHHHHCH	34.49	-
497	Phosphorylation	EKFPEFCSSPSPPVE HHCHHHHCCCCCCCE	51.08	23984901
498	Phosphorylation	KFPEFCSSPSPPVEV HCHHHHCCCCCCCEE	30.49	27566939
500	Phosphorylation	PEFCSSPSPPVEVKI HHHHCCCCCCCEEEE	43.73	25521595
512	Phosphorylation	VKIEEPVSMEMDNHL EEECCCCCCCCCCCC	21.53	25293948
520	Phosphorylation	MEMDNHLSDKDESCY CCCCCCCCCCCCCHH	34.75	25159016
525	Phosphorylation	HLSDKDESCYDNAEA CCCCCCCCHHHCHHH	28.27	23984901
527	Phosphorylation	SDKDESCYDNAEAAF CCCCCCHHHCHHHHC	22.85	23984901
535	Phosphorylation	DNAEAAFSDDEEDLN HCHHHHCCCCHHHHH	39.15	25521595
543	Phosphorylation	DDEEDLNSKGKKREF CCHHHHHHCCCCCCE	50.51	23984901
896	Ubiquitination	HIKALLIKNNSLPRK HHHHHHHHCCCCCHH	50.47	22790023
906	Phosphorylation	SLPRKRQSLRSSSSK CCCHHHHHHHCCHHH	29.77	-
913	Ubiquitination	SLRSSSSKLAQLTLE HHHCCHHHHHHHHHH	50.19	-
992	Phosphorylation	SRRKAALSSPRSRKN HHHHHHHCCCCHHCC	33.30	28833060
993	Phosphorylation	RRKAALSSPRSRKNA HHHHHHCCCCHHCCC	25.78	27149854
996	Phosphorylation	AALSSPRSRKNATQP HHHCCCCHHCCCCCC	51.49	22817900
1001	Phosphorylation	PRSRKNATQPPNAEE CCHHCCCCCCCCCCC	51.51	21149613
1010	Phosphorylation	PPNAEEESGSSSASE CCCCCCCCCCCCCCC	47.45	21149613
1012	Phosphorylation	NAEEESGSSSASEEE CCCCCCCCCCCCCCC	30.33	21149613
1013	Phosphorylation	AEEESGSSSASEEED CCCCCCCCCCCCCCC	33.19	21149613
1014	Phosphorylation	EEESGSSSASEEEDT CCCCCCCCCCCCCCC	37.20	21149613
1016	Phosphorylation	ESGSSSASEEEDTKP CCCCCCCCCCCCCCC	47.70	21149613
1021	Phosphorylation	SASEEEDTKPKPTKR CCCCCCCCCCCCCCC	53.15	29550500
1026	Phosphorylation	EDTKPKPTKRKRKGS CCCCCCCCCCCCCCC	50.00	21149613
1033	Phosphorylation	TKRKRKGSSAVGSDS CCCCCCCCCCCCCCC	20.40	22817900
1034	Phosphorylation	KRKRKGSSAVGSDSD CCCCCCCCCCCCCCC	35.33	23684622
1038	Phosphorylation	KGSSAVGSDSD---- CCCCCCCCCCC----	27.61	27087446
1040	Phosphorylation	SSAVGSDSD------ CCCCCCCCC------	47.09	27087446

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

Oops, there are no upstream regulatory protein records of INT3_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of INT3_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of INT3_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of INT3_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1038 AND SER-1040, ANDMASS SPECTROMETRY.
PubMed: 19367708