dbPTM

ADDA_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ADDA_MOUSE
UniProt AC	Q9QYC0
Protein Name	Alpha-adducin
Gene Name	Add1
Organism	Mus musculus (Mouse).
Sequence Length	735
Subcellular Localization	Cytoplasm, cytoskeleton. Cell membrane Peripheral membrane protein Cytoplasmic side.
Protein Description	Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Binds to calmodulin..
Protein Sequence	MNGDTRAAVVTSPPPTTAPHKERYFDRVDENNPEYLRERNMAPDLRQDFNMMEQKKRVSMILQSPAFCEELESMIQEQFKKGKNPTGLLALQQIADFMTASVPNVYPAAPQGGMAALNMSLGMVTPVNDLRGSDSIAYDKGEKLLRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKVNLQGDIVDRGSTNLGVNQAGFTLHSAVYAARPDAKCIVHIHTPAGAAVSAMKCGLLPISPEALSLGDVAYHDYHGILVDEEEKILIQKNLGPKSKVLILRNHGLVSVGESVEEAFYYIHNLVVACEIQVRTLASAGGPDNLVLLDPGKYKAKSRSPGTPAGEGSGSPPKWQIGEQEFEALMRMLDNLGYRTGYPYRYPALRERSKKYSDVEVPASVTGHSFASDGDSGTCSPLRHSFQKQQREKTRWLHSGRGDDASEEGQNGSSPKSKTKWTKEDGHRTSTSAVPNLFVPLNTNPKEVQEMRNKIREQNLQDIKTAGPQSQVLCGVMMDRSLVQGELVTASKAIIEKEYQPHVIVSTTGPNPFNTLTDRELEEYRREVERKQKGSEENLDETREQKEKSPPDQSAVPNTPPSTPVKLEEDLPQEPTSRDDSDATTFKPTPPDLSPDEPSEALAFPAVEEEAHASPDPTQPPAEADPEPASAPTPGAEEVASPATEEGSPMDPGSDGSPGKSPSKKKKKFRTPSFLKKSKKKSDS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MNGDTRAA -------CCCCCEEE	13.11	-
11	O-linked_Glycosylation	DTRAAVVTSPPPTTA CCEEEEECCCCCCCC	28.99	22645316
11	Phosphorylation	DTRAAVVTSPPPTTA CCEEEEECCCCCCCC	28.99	25521595
12	Phosphorylation	TRAAVVTSPPPTTAP CEEEEECCCCCCCCC	24.65	24925903
16	Phosphorylation	VVTSPPPTTAPHKER EECCCCCCCCCCHHH	41.17	24925903
16	O-linked_Glycosylation	VVTSPPPTTAPHKER EECCCCCCCCCCHHH	41.17	22645316
17	Phosphorylation	VTSPPPTTAPHKERY ECCCCCCCCCCHHHH	43.92	24925903
17	O-linked_Glycosylation	VTSPPPTTAPHKERY ECCCCCCCCCCHHHH	43.92	22645316
21	Ubiquitination	PPTTAPHKERYFDRV CCCCCCCHHHHHCCC	42.71	-
35	Phosphorylation	VDENNPEYLRERNMA CCCCCHHHHHHHCCC	16.59	62921
59	Phosphorylation	MEQKKRVSMILQSPA HHHHHHHHHHHHCHH	12.25	28978645
64	Phosphorylation	RVSMILQSPAFCEEL HHHHHHHCHHHHHHH	18.10	16285637
133	Phosphorylation	PVNDLRGSDSIAYDK CHHHCCCCCCCCCCC	23.04	28285833
135	Phosphorylation	NDLRGSDSIAYDKGE HHCCCCCCCCCCCCC	15.71	25521595
138	Phosphorylation	RGSDSIAYDKGEKLL CCCCCCCCCCCCHHH	19.27	29899451
148	Ubiquitination	GEKLLRCKLAAFYRL CCHHHHHHHHHHHHH	34.42	-
288	Ubiquitination	EEKILIQKNLGPKSK HHHHHEECCCCCCCE	47.34	-
288	Acetylation	EEKILIQKNLGPKSK HHHHHEECCCCCCCE	47.34	22826441
331	Phosphorylation	ACEIQVRTLASAGGP EEEEEHHHHHHCCCC	28.02	-
334	Phosphorylation	IQVRTLASAGGPDNL EEHHHHHHCCCCCCE	30.47	-
353	Phosphorylation	PGKYKAKSRSPGTPA CCCCEECCCCCCCCC	42.73	25521595
355	Phosphorylation	KYKAKSRSPGTPAGE CCEECCCCCCCCCCC	34.47	25521595
358	Phosphorylation	AKSRSPGTPAGEGSG ECCCCCCCCCCCCCC	17.22	25521595
364	Phosphorylation	GTPAGEGSGSPPKWQ CCCCCCCCCCCCCCC	31.62	25521595
366	Phosphorylation	PAGEGSGSPPKWQIG CCCCCCCCCCCCCCC	39.46	25521595
397	Phosphorylation	RTGYPYRYPALRERS CCCCCCCCHHHHHHH	6.24	28576409
404	Phosphorylation	YPALRERSKKYSDVE CHHHHHHHCCCCCCC	28.84	28576409
407	Phosphorylation	LRERSKKYSDVEVPA HHHHHCCCCCCCCCC	17.53	25619855
408	Phosphorylation	RERSKKYSDVEVPAS HHHHCCCCCCCCCCH	44.02	25521595
415	Phosphorylation	SDVEVPASVTGHSFA CCCCCCCHHCCCCCC	17.72	24925903
417	Phosphorylation	VEVPASVTGHSFASD CCCCCHHCCCCCCCC	27.04	24925903
420	Phosphorylation	PASVTGHSFASDGDS CCHHCCCCCCCCCCC	24.69	24925903
423	Phosphorylation	VTGHSFASDGDSGTC HCCCCCCCCCCCCCC	39.87	24925903
427	Phosphorylation	SFASDGDSGTCSPLR CCCCCCCCCCCCCCH	41.34	25521595
429	Phosphorylation	ASDGDSGTCSPLRHS CCCCCCCCCCCCHHH	17.48	25521595
430	S-nitrosylation	SDGDSGTCSPLRHSF CCCCCCCCCCCHHHH	4.50	24895380
431	Phosphorylation	DGDSGTCSPLRHSFQ CCCCCCCCCCHHHHH	27.14	25521595
436	Phosphorylation	TCSPLRHSFQKQQRE CCCCCHHHHHHHHHH	23.96	27087446
445	Phosphorylation	QKQQREKTRWLHSGR HHHHHHHHHHCCCCC	23.48	26643407
450	Phosphorylation	EKTRWLHSGRGDDAS HHHHHCCCCCCCCCC	28.19	25619855
457	Phosphorylation	SGRGDDASEEGQNGS CCCCCCCCCCCCCCC	43.08	25619855
464	Phosphorylation	SEEGQNGSSPKSKTK CCCCCCCCCCCCCCC	51.52	25521595
465	Phosphorylation	EEGQNGSSPKSKTKW CCCCCCCCCCCCCCC	37.43	25521595
468	Phosphorylation	QNGSSPKSKTKWTKE CCCCCCCCCCCCCCC	49.28	25367039
480	Phosphorylation	TKEDGHRTSTSAVPN CCCCCCCCCCCCCCC	30.59	27742792
481	Phosphorylation	KEDGHRTSTSAVPNL CCCCCCCCCCCCCCE	21.96	27742792
482	Phosphorylation	EDGHRTSTSAVPNLF CCCCCCCCCCCCCEE	21.79	27742792
483	Phosphorylation	DGHRTSTSAVPNLFV CCCCCCCCCCCCEEE	27.34	27742792
497	Ubiquitination	VPLNTNPKEVQEMRN ECCCCCHHHHHHHHH	73.00	-
525	S-nitrosylation	GPQSQVLCGVMMDRS CCHHHHHHHHCCCCC	3.97	22178444
525	S-nitrosocysteine	GPQSQVLCGVMMDRS CCHHHHHHHHCCCCC	3.97	-
532	Phosphorylation	CGVMMDRSLVQGELV HHHCCCCCHHCCCEE	28.73	22817900
540	O-linked_Glycosylation	LVQGELVTASKAIIE HHCCCEEECCHHHHH	37.53	22645316
542	O-linked_Glycosylation	QGELVTASKAIIEKE CCCEEECCHHHHHHH	17.16	55410791
550	Phosphorylation	KAIIEKEYQPHVIVS HHHHHHHHCCCEEEE	38.11	6822601
557	O-linked_Glycosylation	YQPHVIVSTTGPNPF HCCCEEEECCCCCCC	14.77	22645316
558	O-linked_Glycosylation	QPHVIVSTTGPNPFN CCCEEEECCCCCCCC	25.52	22645316
559	O-linked_Glycosylation	PHVIVSTTGPNPFNT CCEEEECCCCCCCCC	43.04	22645316
566	Phosphorylation	TGPNPFNTLTDRELE CCCCCCCCCCHHHHH	31.26	29899451
586	Phosphorylation	VERKQKGSEENLDET HHHHHCCCCCCHHHH	49.09	25521595
593	Phosphorylation	SEENLDETREQKEKS CCCCHHHHHHHHHHC	38.89	25521595
600 (in isoform 2)	Phosphorylation	-	42.64	22807455
600	Phosphorylation	TREQKEKSPPDQSAV HHHHHHHCCCCCCCC	42.64	25521595
605	Phosphorylation	EKSPPDQSAVPNTPP HHCCCCCCCCCCCCC	38.32	25521595
605 (in isoform 2)	Phosphorylation	-	38.32	26745281
610	Phosphorylation	DQSAVPNTPPSTPVK CCCCCCCCCCCCCCC	30.42	24925903
610 (in isoform 2)	Phosphorylation	-	30.42	25521595
613	Phosphorylation	AVPNTPPSTPVKLEE CCCCCCCCCCCCCCC	46.69	24925903
613 (in isoform 2)	Phosphorylation	-	46.69	25521595
614 (in isoform 2)	Phosphorylation	-	37.56	25266776
614	Phosphorylation	VPNTPPSTPVKLEED CCCCCCCCCCCCCCC	37.56	24925903
627	Phosphorylation	EDLPQEPTSRDDSDA CCCCCCCCCCCCCCC	35.32	24925903
628	Phosphorylation	DLPQEPTSRDDSDAT CCCCCCCCCCCCCCC	44.41	25521595
640	Phosphorylation	DATTFKPTPPDLSPD CCCCCCCCCCCCCCC	48.30	21082442
645	Phosphorylation	KPTPPDLSPDEPSEA CCCCCCCCCCCCCHH	37.37	21082442
665	Phosphorylation	VEEEAHASPDPTQPP HHHHHHCCCCCCCCC	21.70	25338131
705	Phosphorylation	GSPMDPGSDGSPGKS CCCCCCCCCCCCCCC	44.16	25338131
708	Phosphorylation	MDPGSDGSPGKSPSK CCCCCCCCCCCCCCH	35.15	25338131
712	Phosphorylation	SDGSPGKSPSKKKKK CCCCCCCCCCHHHCC	40.08	25338131
714	Phosphorylation	GSPGKSPSKKKKKFR CCCCCCCCHHHCCCC	65.29	25338131
722	Phosphorylation	KKKKKFRTPSFLKKS HHHCCCCCHHHHHHH	26.81	27742792
724	Phosphorylation	KKKFRTPSFLKKSKK HCCCCCHHHHHHHHC	42.47	25521595
729	Phosphorylation	TPSFLKKSKKKSDS- CHHHHHHHHCCCCC-	48.39	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
445	T	Phosphorylation	Kinase	ROCK2	P70336	Uniprot
480	T	Phosphorylation	Kinase	ROCK2	P70336	Uniprot
481	S	Phosphorylation	Kinase	PKA	-	Uniprot
714	S	Phosphorylation	Kinase	PKC	-	Uniprot
724	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
724	S	Phosphorylation	Kinase	PKA	-	Uniprot
724	S	Phosphorylation	Kinase	PKC	-	Uniprot

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMCA4_MOUSE	Smarca4	physical	17074803
SMRC1_MOUSE	Smarcc1	physical	17074803
SIN3A_MOUSE	Sin3a	physical	17074803

Drug and Disease Associations

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

Regulatory Network of ADDA_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 THR-358; SER-483 ANDTHR-610, AND MASS SPECTROMETRY.	17242355 [Abstract]
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355; THR-358; SER-586;THR-610 AND THR-614, AND MASS SPECTROMETRY.	17114649 [Abstract]
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations."; Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.; Mol. Cell. Proteomics 5:914-922(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-586, AND MASSSPECTROMETRY.	16452087 [Abstract]
"Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-610, AND MASSSPECTROMETRY.	15345747 [Abstract]