dbPTM

DIP2B_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DIP2B_MOUSE
UniProt AC	Q3UH60
Protein Name	Disco-interacting protein 2 homolog B
Gene Name	Dip2b
Organism	Mus musculus (Mouse).
Sequence Length	1574
Subcellular Localization
Protein Description
Protein Sequence	MAERGLEPSPAAVAALPPEVRAQLAELELELSEGDITQKGYEKKRSKLLSPYSPQTQETDSIGQKERNQTPAPTAAQTSAPSKYHRSRSGGARDERYRSDIHTEAVQAALAKHKEQKMALPMPTKRRSTFVQSPADACTPPDTSSASEDEGSLRRQAALSAALQQSLQNAESWINRSIQGSSTSSSASSTLSHGEVKGTSGSLADVFANTRIENVSAPPDVTATTSSSSSSLRPANIDLPPSGIVKGMHKGSNRSSLMDTADGVPVNSRVSTKIQQLLNTLKRPKRPPLKEFFVDDSEEIVEGIPQPDPNQPKPEGRQMTPVKGEPLGVICNWPPALESALQRWGSTQAKCPCLTGLDVTGKPVYTLTYGKLWSRSLKLAYTLLNKLGTKNEPVLKPGDRVALVYPNNDPVMFMVAFYGCLLAEVIPVPIEVPLTRKDAGGQQIGFLLGSCGIALALTSEICLKGLPKTQNGEIVQFKGWPRLKWVVTDSKYLSKPPKDWQPHISPAGTEPAYIEYKTSKEGSVMGVTVSRLAMLSQCQALSQACNYSEGETVVNVLDFKKDAGLWHGMFANVMNKMHTISVPYSVMKTCPLSWVQRVHAHKAKVALVKCRDLHWAMMAHRDQRDVSLSSLRMLIVTDGANPWSVSSCDAFLSLFQSHGLKPEAICPCATSAEAMTVAIRRPGVPGAPLPGRAILSMNGLSYGVIRVNTEDKNSALTVQDVGHVMPGGMMCIVKPDGLPQLCRTDEIGEICVSSRTGGMMYFGLAGVTKNTFEVIPVTSSGSPVGDVPFIRSGLLGFVGPGSLVFVVGKMDGLLMVSGRRHNADDIVATGLAVESIKTVYRGRIAVFSVSVFYDERIVVVAEQRPDASEEDSFQWMSRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGIHISQTKQLFLEGSLHPCNILMCPHTCVTNLPKPRQKQPGVGPASVMVGNLVAGKRIAQAAGRDLGQIEENDLVRKHQFLAEILQWRAQATPDHVLFMLLNAKGTTVCTASCLQLHKRAERIASVLGDKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPPHAQNLTATLPTVRMVVDVSKAACVLTTQTLMRLLKSREAAAAVDVKTWPAIIDTDDLPRKRLPQLYKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAIKLQCELYSSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLIPPMELENNLFLWLATVNQYKIRDTFCSYSVMELCTKGLGNQVEVLKTRGINLSCIRTCVVVAEERPRVSLQQSFSKLFKDIGLSPRAVSTTFGSRVNVAICLQGTSGPDPTTVYVDLKSLRHDRVRLVERGAPQSLLLSESGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTASGYYTIYDSETLQADHFNTRLSFGDAAQTLWARTGYLGFVRRTELTAATGERHDALYVVGALDETLELRGLRYHPIDIETSVSRVHRSIAECAVFTWTNLLVVVVELCGSEQEALDLVPLVTNVVLEEHYLIVGVVVVVDPGVVPINSRGEKQRMHLRDSFLADQLDPIYVAYNM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Phosphorylation	AERGLEPSPAAVAAL CCCCCCCCHHHHHCC	20.14	26824392
47	Ubiquitination	GYEKKRSKLLSPYSP CHHHHHHHCCCCCCC	58.44	22790023
50	Phosphorylation	KKRSKLLSPYSPQTQ HHHHHCCCCCCCCCC	32.03	26745281
52	Phosphorylation	RSKLLSPYSPQTQET HHHCCCCCCCCCCCC	29.61	29899451
53	Phosphorylation	SKLLSPYSPQTQETD HHCCCCCCCCCCCCC	17.57	26745281
56	Phosphorylation	LSPYSPQTQETDSIG CCCCCCCCCCCCCCC	31.58	29899451
59	Phosphorylation	YSPQTQETDSIGQKE CCCCCCCCCCCCCCC	25.81	26745281
61	Phosphorylation	PQTQETDSIGQKERN CCCCCCCCCCCCCCC	35.72	30352176
65	Ubiquitination	ETDSIGQKERNQTPA CCCCCCCCCCCCCCC	54.12	22790023
70	Phosphorylation	GQKERNQTPAPTAAQ CCCCCCCCCCCCCCC	25.60	23684622
74	Phosphorylation	RNQTPAPTAAQTSAP CCCCCCCCCCCCCCC	36.41	28066266
78	Phosphorylation	PAPTAAQTSAPSKYH CCCCCCCCCCCCCCC	23.33	23684622
79	Phosphorylation	APTAAQTSAPSKYHR CCCCCCCCCCCCCCC	26.54	29550500
82	Phosphorylation	AAQTSAPSKYHRSRS CCCCCCCCCCCCCCC	45.63	25777480
89	Phosphorylation	SKYHRSRSGGARDER CCCCCCCCCCCCCHH	42.71	-
97	Phosphorylation	GGARDERYRSDIHTE CCCCCHHHHHHHHHH	16.66	25521595
99	Phosphorylation	ARDERYRSDIHTEAV CCCHHHHHHHHHHHH	31.79	26824392
103	Phosphorylation	RYRSDIHTEAVQAAL HHHHHHHHHHHHHHH	26.44	22817900
128	Phosphorylation	PMPTKRRSTFVQSPA CCCCCCCCCCCCCHH	30.17	25619855
129	Phosphorylation	MPTKRRSTFVQSPAD CCCCCCCCCCCCHHH	26.47	25619855
133	Phosphorylation	RRSTFVQSPADACTP CCCCCCCCHHHHCCC	19.43	25619855
139	Phosphorylation	QSPADACTPPDTSSA CCHHHHCCCCCCCCC	39.31	25619855
143	Phosphorylation	DACTPPDTSSASEDE HHCCCCCCCCCCCCC	30.29	25619855
144	Phosphorylation	ACTPPDTSSASEDEG HCCCCCCCCCCCCCC	31.15	25619855
145	Phosphorylation	CTPPDTSSASEDEGS CCCCCCCCCCCCCCH	37.60	21082442
147	Phosphorylation	PPDTSSASEDEGSLR CCCCCCCCCCCCHHH	47.75	21082442
152	Phosphorylation	SASEDEGSLRRQAAL CCCCCCCHHHHHHHH	19.36	21082442
177	Phosphorylation	AESWINRSIQGSSTS HHHHHHHHHCCCCCC	18.12	26643407
181	Phosphorylation	INRSIQGSSTSSSAS HHHHHCCCCCCCCCC	17.67	26643407
182	Phosphorylation	NRSIQGSSTSSSASS HHHHCCCCCCCCCCC	38.85	26643407
183	Phosphorylation	RSIQGSSTSSSASST HHHCCCCCCCCCCCC	34.03	24759943
184	Phosphorylation	SIQGSSTSSSASSTL HHCCCCCCCCCCCCC	25.01	26643407
185	Phosphorylation	IQGSSTSSSASSTLS HCCCCCCCCCCCCCC	29.97	24759943
186	Phosphorylation	QGSSTSSSASSTLSH CCCCCCCCCCCCCCC	31.75	26643407
188	Phosphorylation	SSTSSSASSTLSHGE CCCCCCCCCCCCCCE	26.29	26643407
189	Phosphorylation	STSSSASSTLSHGEV CCCCCCCCCCCCCEE	32.84	26643407
190	Phosphorylation	TSSSASSTLSHGEVK CCCCCCCCCCCCEEC	29.77	26643407
192	Phosphorylation	SSASSTLSHGEVKGT CCCCCCCCCCEECCC	29.54	26643407
199	Phosphorylation	SHGEVKGTSGSLADV CCCEECCCCCCHHHH	24.97	26643407
200	Phosphorylation	HGEVKGTSGSLADVF CCEECCCCCCHHHHH	34.74	26824392
202	Phosphorylation	EVKGTSGSLADVFAN EECCCCCCHHHHHCC	21.83	25521595
210	Phosphorylation	LADVFANTRIENVSA HHHHHCCCCEEECCC	29.60	25777480
252	Phosphorylation	VKGMHKGSNRSSLMD CCCCCCCCCCCCCCC	33.60	25521595
255	Phosphorylation	MHKGSNRSSLMDTAD CCCCCCCCCCCCCCC	31.88	26643407
256	Phosphorylation	HKGSNRSSLMDTADG CCCCCCCCCCCCCCC	25.19	25266776
260	Phosphorylation	NRSSLMDTADGVPVN CCCCCCCCCCCCCCC	16.81	26643407
273	Ubiquitination	VNSRVSTKIQQLLNT CCHHHHHHHHHHHHH	30.89	22790023
280	Phosphorylation	KIQQLLNTLKRPKRP HHHHHHHHCCCCCCC	33.36	26824392
290	Ubiquitination	RPKRPPLKEFFVDDS CCCCCCCHHCCCCCH	59.24	-
320	Phosphorylation	KPEGRQMTPVKGEPL CCCCCCCCCCCCCEE	19.32	22817900
478	Ubiquitination	NGEIVQFKGWPRLKW CCCEEEECCCCCEEE	42.87	22790023
627	Phosphorylation	HRDQRDVSLSSLRML CCCCCCCCHHHEEEE	27.16	23737553
629	Phosphorylation	DQRDVSLSSLRMLIV CCCCCCHHHEEEEEE	21.59	25159016
630	Phosphorylation	QRDVSLSSLRMLIVT CCCCCHHHEEEEEEC	25.86	23737553
692	Methylation	PGAPLPGRAILSMNG CCCCCCCCEEEEECC	19.26	-
778	Phosphorylation	TFEVIPVTSSGSPVG EEEEEEECCCCCCCC	16.30	20415495
779	Phosphorylation	FEVIPVTSSGSPVGD EEEEEECCCCCCCCC	32.70	29899451
780	Phosphorylation	EVIPVTSSGSPVGDV EEEEECCCCCCCCCC	33.65	20415495
782	Phosphorylation	IPVTSSGSPVGDVPF EEECCCCCCCCCCCC	20.54	22817900
964	Ubiquitination	VGNLVAGKRIAQAAG CCHHHHHHHHHHHHC	30.78	22790023
1295	Phosphorylation	PRVSLQQSFSKLFKD CCCCHHHHHHHHHHH	20.66	25338131
1298	Ubiquitination	SLQQSFSKLFKDIGL CHHHHHHHHHHHHCC	56.80	22790023
1306	Phosphorylation	LFKDIGLSPRAVSTT HHHHHCCCCCEECCC	13.71	24759943
1312	Phosphorylation	LSPRAVSTTFGSRVN CCCCEECCCCCCCEE	21.39	25777480
1327	Phosphorylation	VAICLQGTSGPDPTT EEEEECCCCCCCCCE	19.97	25777480
1333	Phosphorylation	GTSGPDPTTVYVDLK CCCCCCCCEEEEEHH	35.95	25777480
1341	Phosphorylation	TVYVDLKSLRHDRVR EEEEEHHHHCCCEEE	37.62	25777480
1365	Ubiquitination	LLLSESGKILPGVKV EEECCCCCCCCCCEE	50.80	22790023
1428	Phosphorylation	SFGDAAQTLWARTGY CHHHHHHHHHHHHCC	21.38	22817900

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
Oops, there are no upstream regulatory protein records of DIP2B_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DIP2B_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 DIP2B_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of DIP2B_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of DIP2B_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-99, AND MASSSPECTROMETRY.	19367708 [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-99; SER-152 AND SER-202,AND MASS SPECTROMETRY.	17242355 [Abstract]