dbPTM

ASPP2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ASPP2_MOUSE
UniProt AC	Q8CG79
Protein Name	Apoptosis-stimulating of p53 protein 2
Gene Name	Tp53bp2
Organism	Mus musculus (Mouse).
Sequence Length	1128
Subcellular Localization	Cytoplasm, perinuclear region. Nucleus. Predominantly found in the perinuclear region. Some small fraction is nuclear..
Protein Description	Regulator that plays a central role in regulation of apoptosis and cell growth via its interactions. Regulates p53/TP53 by enhancing the DNA binding and transactivation function of p53/TP53 on the promoters of proapoptotic genes in vivo. Inhibits the ability of APPBP1 to conjugate NEDD8 to CUL1, and thereby decreases APPBP1 ability to induce apoptosis. Impedes cell cycle progression at G2/M. Its apoptosis-stimulating activity is inhibited by its interaction with DDX42 (By similarity)..
Protein Sequence	MMPMFLTVYLSNSEQHFTEVPVTPETICRDVVDLCKEPGENDCHLAEVWCGSERPVADNERMFDVLQRFGSQRNEVRFFLRHERPPNRDIVSGPRSQDPSVKRNGVKVPGEHRRKENGVNSPRLDLTLAELQEMASRQQQQIEAQQQMLATKEQRLKFLKQQDQRQQQQAAEQEKLKRLREIAESQEAKLKKVRALKGHVEQKRLSNGKLVEEIEQMNSLFQQKQRELVLAVSKVEELTRQLEMLKNGRIDGHHDNQSAVAELDRLYKELQLRNKLNQEQNAKLQQQRECLNKRNSEVAVMDKRVSELRDRLWKKKAALQQKENLPVSPDGNLPQQAVSAPSRVAAVGPYIQSSTMPRMPSRPELLVKPALPDGSLLMQSAEGPMKIQTLPNMRSGAASQSKGSKAHPASPDWNPSNADLLPSQGSSVPQSAGTALDQVDDGEIAVREKEKKVRPFSMFDTVDQCAAPPSFGTLRKNQSSEDILRDAQAVNKNVAKVPPPVPTKPKQIHLPYFGQTAQSPSDMKPDGNAQQLPIAATSVGAKLKPAGPQARMLLSPGAPSGGQDQVLSPASKQESPPAAAVRPFTPQPSKDTFPPAFRKPQTVAASSIYSMYTQQQAPGKNFQQAVQSALTKTQPRGPHFSSVYGKPVIAAAQNPQQHPENIYSCSQGKPGSPEPETETVSSVHESHENERIPRPLSPTKLLPFLSNPYRNQSDADLEALRKKLSNAPRPLKKRSSITEPEGPNGPNIQKLLYQRTTIAAMETISVPSHPSKSPGSVTVNPESSVEIPNPYLHVEPEKEVGSLVPEPLSPEDMGSASTENSDVPAPSAGLEYVSEGVTDSSTNLQNNVEETNPEAPHLLEVYLEEYPPYPPPPYPSGEPEVSEEDSARMRPPEITGQVSLPPGKRTNLRKTGSERIAHGMRVKFNPLALLLDSSLEGEFDLVQRIIYEVDDPSLPNDEGITALHNAVCAGHTEIVKFLVQFGVNVNAADSDGWTPLHCAASCNNVQVCKFLVESGAAVFAMTYSDMQTAADKCEEMEEGYTQCSQFLYGVQEKMGIMNKGVIYALWDYEPQHDDELLMKEGDCMTVIRREDEEEIEWWWARLNDKEGYVPRNLLGLYPRIKPRQRSLA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
92	Phosphorylation	PPNRDIVSGPRSQDP CCCCCCCCCCCCCCC	43.33	25777480
121	Phosphorylation	RKENGVNSPRLDLTL CHHCCCCCCHHHHHH	14.70	101544657
127	Phosphorylation	NSPRLDLTLAELQEM CCCHHHHHHHHHHHH	24.48	23984901
136	Phosphorylation	AELQEMASRQQQQIE HHHHHHHHHHHHHHH	29.34	23984901
185	O-linked_Glycosylation	RLREIAESQEAKLKK HHHHHHHHHHHHHHH	25.05	30059200
206	Phosphorylation	HVEQKRLSNGKLVEE HHHHHCCCCCCHHHH	47.79	26745281
212	Phosphorylation	LSNGKLVEEIEQMNS CCCCCHHHHHHHHHH	64.79	24719451
296	Phosphorylation	ECLNKRNSEVAVMDK HHHHHHCCHHHHHHH	37.16	25266776
306	Phosphorylation	AVMDKRVSELRDRLW HHHHHHHHHHHHHHH	34.64	27149854
328	Phosphorylation	QKENLPVSPDGNLPQ HHHCCCCCCCCCCCH	18.48	27087446
339	O-linked_Glycosylation	NLPQQAVSAPSRVAA CCCHHHHCCCCCEEE	37.16	30059200
350	Phosphorylation	RVAAVGPYIQSSTMP CEEECCCCCCCCCCC	12.98	29514104
355	Phosphorylation	GPYIQSSTMPRMPSR CCCCCCCCCCCCCCC	36.12	29514104
361	Phosphorylation	STMPRMPSRPELLVK CCCCCCCCCCCCEEE	51.64	26643407
389	Phosphorylation	EGPMKIQTLPNMRSG CCCCEEECCCCCCCC	47.89	22006019
410	Phosphorylation	GSKAHPASPDWNPSN CCCCCCCCCCCCHHH	28.04	25619855
416	Phosphorylation	ASPDWNPSNADLLPS CCCCCCHHHCCCCCC	41.24	25619855
423	Phosphorylation	SNADLLPSQGSSVPQ HHCCCCCCCCCCCCC	47.33	25619855
426	Phosphorylation	DLLPSQGSSVPQSAG CCCCCCCCCCCCCCC	22.11	25619855
427	Phosphorylation	LLPSQGSSVPQSAGT CCCCCCCCCCCCCCC	44.64	25619855
457	Phosphorylation	EKKVRPFSMFDTVDQ CCCCCCCCCCCCHHH	22.63	21585329
479	Phosphorylation	GTLRKNQSSEDILRD CCCCCCCCHHHHHHH	45.12	26824392
480	Phosphorylation	TLRKNQSSEDILRDA CCCCCCCHHHHHHHH	29.53	23429704
485	Phosphorylation	QSSEDILRDAQAVNK CCHHHHHHHHHHHCC	37.24	24719451
503	Phosphorylation	KVPPPVPTKPKQIHL CCCCCCCCCCCEECC	61.28	51456803
555	Phosphorylation	PQARMLLSPGAPSGG HHCEEEECCCCCCCC	19.82	26643407
560	Phosphorylation	LLSPGAPSGGQDQVL EECCCCCCCCCCCCC	55.83	26643407
568	Phosphorylation	GGQDQVLSPASKQES CCCCCCCCCCCCCCC	21.40	26643407
571	Phosphorylation	DQVLSPASKQESPPA CCCCCCCCCCCCCCC	37.95	26643407
575	Phosphorylation	SPASKQESPPAAAVR CCCCCCCCCCCCCCC	33.42	37816809
585	Phosphorylation	AAAVRPFTPQPSKDT CCCCCCCCCCCCCCC	24.56	26643407
589	Phosphorylation	RPFTPQPSKDTFPPA CCCCCCCCCCCCCCH	37.61	26643407
609	Phosphorylation	TVAASSIYSMYTQQQ HHHHHHHHHHHHCCC	6.85	18563927
641	Phosphorylation	QPRGPHFSSVYGKPV CCCCCCCHHHCCCCE	18.83	25367039
642	Phosphorylation	PRGPHFSSVYGKPVI CCCCCCHHHCCCCEE	20.58	25367039
644	Phosphorylation	GPHFSSVYGKPVIAA CCCCHHHCCCCEEEE	22.75	25367039
663	Phosphorylation	QQHPENIYSCSQGKP CCCCCCCCCCCCCCC	18.40	22529
664	Phosphorylation	QHPENIYSCSQGKPG CCCCCCCCCCCCCCC	11.96	25367039
666	Phosphorylation	PENIYSCSQGKPGSP CCCCCCCCCCCCCCC	35.71	25367039
672	Phosphorylation	CSQGKPGSPEPETET CCCCCCCCCCCCCCC	34.32	21149613
677	Phosphorylation	PGSPEPETETVSSVH CCCCCCCCCCCCCCC	47.90	25367039
679	Phosphorylation	SPEPETETVSSVHES CCCCCCCCCCCCCHH	32.86	25367039
681	Phosphorylation	EPETETVSSVHESHE CCCCCCCCCCCHHHC	33.78	25367039
682	Phosphorylation	PETETVSSVHESHEN CCCCCCCCCCHHHCC	24.13	25367039
686	Phosphorylation	TVSSVHESHENERIP CCCCCCHHHCCCCCC	22.63	25367039
697	Phosphorylation	ERIPRPLSPTKLLPF CCCCCCCCHHHHHHC	32.95	25521595
699	Phosphorylation	IPRPLSPTKLLPFLS CCCCCCHHHHHHCCC	30.83	14207685
713	Phosphorylation	SNPYRNQSDADLEAL CCCCCCCCHHHHHHH	38.01	17242355
725	Phosphorylation	EALRKKLSNAPRPLK HHHHHHHHCCCCCCC	39.56	51456811
735	Phosphorylation	PRPLKKRSSITEPEG CCCCCCCCCCCCCCC	34.66	25521595
736	Phosphorylation	RPLKKRSSITEPEGP CCCCCCCCCCCCCCC	37.25	25521595
738	Phosphorylation	LKKRSSITEPEGPNG CCCCCCCCCCCCCCC	47.65	21082442
756	Phosphorylation	QKLLYQRTTIAAMET HHHHHHHHHEEEEEE	13.66	26026062
763	Phosphorylation	TTIAAMETISVPSHP HHEEEEEEEECCCCC	12.88	26026062
791	Phosphorylation	SVEIPNPYLHVEPEK CCCCCCCCEECCCCC	18.97	29514104

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
585	T	Phosphorylation	Kinase	MAPK1	P63085	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ASPP2_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of ASPP2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of ASPP2_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of ASPP2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-697, AND MASSSPECTROMETRY.	19131326 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479, AND MASSSPECTROMETRY.	17242355 [Abstract]