dbPTM

AT2A2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AT2A2_MOUSE
UniProt AC	O55143
Protein Name	Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
Gene Name	Atp2a2
Organism	Mus musculus (Mouse).
Sequence Length	1044
Subcellular Localization	Endoplasmic reticulum membrane Multi-pass membrane protein . Sarcoplasmic reticulum membrane Multi-pass membrane protein .
Protein Description	This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Isoform SERCA2A is involved in the regulation of the contraction/relaxation cycle. Acts as a regulator of TNFSF11-mediated Ca(2+) signaling pathways via its interaction with TMEM64 which is critical for the TNFSF11-induced CREB1 activation and mitochondrial ROS generation necessary for proper osteoclast generation. Association between TMEM64 and SERCA2 in the ER leads to cytosolic Ca (2+) spiking for activation of NFATC1 and production of mitochondrial ROS, thereby triggering Ca (2+) signaling cascades that promote osteoclast differentiation and activation. [PubMed: 23395171]
Protein Sequence	MENAHTKTVEEVLGHFGVNESTGLSLEQVKKLKERWGSNELPAEEGKTLLELVIEQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILVANAIVGVWQERNAENAIEALKEYEPEMGKVYRQDRKSVQRIKAKDIVPGDIVEIAVGDKVPADIRLTSIKSTTLRVDQSILTGESVSVIKHTDPVPDPRAVNQDKKNMLFSGTNIAAGKAMGVVVATGVNTEIGKIRDEMVATEQERTPLQQKLDEFGEQLSKVISLICIAVWIINIGHFNDPVHGGSWIRGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFILDKVEGDTCSLNEFSITGSTYAPIGEVQKDDKPVKCHQYDGLVELATICALCNDSALDYNEAKGVYEKVGEATETALTCLVEKMNVFDTELKGLSKIERANACNSVIKQLMKKEFTLEFSRDRKSMSVYCTPNKPSRTSMSKMFVKGAPEGVIDRCTHIRVGSTKVPMTPGVKQKIMSVIREWGSGSDTLRCLALATHDNPLKREEMHLEDSANFIKYETNLTFVGCVGMLDPPRIEVASSVKLCRQAGIRVIMITGDNKGTAVAICRRIGIFGQDEDVTSKAFTGREFDELSPSAQRDACLNARCFARVEPSHKSKIVEFLQSFDEITAMTGDGVNDAPALKKSEIGIAMGSGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVCIFLTAALGFPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMNKPPRNPKEPLISGWLFFRYLAIGCYVGAATVGAAAWWFIAADGGPRVSFYQLSHFLQCKEDNPDFDGVDCAIFESPYPMTMALSVLVTIEMCNALNSLSENQSLLRMPPWENIWLVGSICLSMSLHFLILYVEPLPLIFQITPLNLTQWLMVLKISLPVILMDETLKFVARNYLEQPGKECVQPATKSSCSLSACTDGISWPFVLLIMPLVVWVYSTDTNFSDMFWS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
38	Phosphorylation	KLKERWGSNELPAEE HHHHHHCCCCCCHHH	21.85	23737553
120	Ubiquitination	ENAIEALKEYEPEMG HHHHHHHHHHCHHHC	66.36	-
122	Phosphorylation	AIEALKEYEPEMGKV HHHHHHHHCHHHCCH	34.89	28464351
128	Ubiquitination	EYEPEMGKVYRQDRK HHCHHHCCHHHCCHH	34.48	-
136	Phosphorylation	VYRQDRKSVQRIKAK HHHCCHHHHHHHHHH	25.11	22324799
143	Ubiquitination	SVQRIKAKDIVPGDI HHHHHHHHHCCCCCE	42.88	17451654
143 (in isoform 2)	Ubiquitination	-	42.88	-
158	Ubiquitination	VEIAVGDKVPADIRL EEEECCCCCCCCEEE	44.16	-
169	Ubiquitination	DIRLTSIKSTTLRVD CEEEEECCCCEEEEE	41.33	-
170	Phosphorylation	IRLTSIKSTTLRVDQ EEEEECCCCEEEEEC	25.59	24719451
181	Phosphorylation	RVDQSILTGESVSVI EEECHHHCCCCEEEE	36.91	27742792
184	Phosphorylation	QSILTGESVSVIKHT CHHHCCCCEEEEECC	22.49	23737553
186	Phosphorylation	ILTGESVSVIKHTDP HHCCCCEEEEECCCC	27.66	23737553
189	Ubiquitination	GESVSVIKHTDPVPD CCCEEEEECCCCCCC	37.99	-
191	Phosphorylation	SVSVIKHTDPVPDPR CEEEEECCCCCCCCC	36.68	28464351
205	Malonylation	RAVNQDKKNMLFSGT CCCCCCCCCCCCCCC	56.74	32601280
210	Phosphorylation	DKKNMLFSGTNIAAG CCCCCCCCCCCCCCC	40.52	27742792
212	Phosphorylation	KNMLFSGTNIAAGKA CCCCCCCCCCCCCCC	23.42	27742792
294	Nitrated tyrosine	SWIRGAIYYFKIAVA CCHHHHHHHHHHHHH	11.43	-
294	Nitration	SWIRGAIYYFKIAVA CCHHHHHHHHHHHHH	11.43	-
295	Nitrated tyrosine	WIRGAIYYFKIAVAL CHHHHHHHHHHHHHH	7.71	-
295	Nitration	WIRGAIYYFKIAVAL CHHHHHHHHHHHHHH	7.71	-
295	Nitration	WIRGAIYYFKIAVAL CHHHHHHHHHHHHHH	7.71	-
328	Ubiquitination	LGTRRMAKKNAIVRS HCCHHHHHHCHHHHC	36.90	-
335	Phosphorylation	KKNAIVRSLPSVETL HHCHHHHCCCCCCCC	33.46	28464351
338	Phosphorylation	AIVRSLPSVETLGCT HHHHCCCCCCCCCCC	37.57	22210690
341	Phosphorylation	RSLPSVETLGCTSVI HCCCCCCCCCCCEEE	26.71	28464351
345	Phosphorylation	SVETLGCTSVICSDK CCCCCCCCEEEEECC	24.99	28464351
346	Phosphorylation	VETLGCTSVICSDKT CCCCCCCEEEEECCC	17.35	28542873
353	Phosphorylation	SVICSDKTGTLTTNQ EEEEECCCCCCCCCC	40.15	24719451
357	Phosphorylation	SDKTGTLTTNQMSVC ECCCCCCCCCCCCEE	24.44	24719451
358	Phosphorylation	DKTGTLTTNQMSVCR CCCCCCCCCCCCEEE	26.94	21082442
364	S-nitrosocysteine	TTNQMSVCRMFILDK CCCCCCEEEEEEEEE	1.73	-
364	Glutathionylation	TTNQMSVCRMFILDK CCCCCCEEEEEEEEE	1.73	24333276
364	S-nitrosylation	TTNQMSVCRMFILDK CCCCCCEEEEEEEEE	1.73	21278135
364	S-palmitoylation	TTNQMSVCRMFILDK CCCCCCEEEEEEEEE	1.73	28526873
376	Phosphorylation	LDKVEGDTCSLNEFS EEECCCCCCCCCEEE	18.17	27742792
377	S-nitrosocysteine	DKVEGDTCSLNEFSI EECCCCCCCCCEEEE	5.32	-
377	S-nitrosylation	DKVEGDTCSLNEFSI EECCCCCCCCCEEEE	5.32	21278135
378	Phosphorylation	KVEGDTCSLNEFSIT ECCCCCCCCCEEEEC	36.00	27742792
383	Phosphorylation	TCSLNEFSITGSTYA CCCCCEEEECCCCEE	17.05	27742792
385	Phosphorylation	SLNEFSITGSTYAPI CCCEEEECCCCEEEC	24.71	27742792
415	Phosphorylation	DGLVELATICALCND CCHHHHHHHHHHHCC	29.25	22817900
427	Phosphorylation	CNDSALDYNEAKGVY HCCCCCCHHHHCCHH	18.76	-
441	Phosphorylation	YEKVGEATETALTCL HHHHHHHHHHHHHHH	29.57	21082442
443	Phosphorylation	KVGEATETALTCLVE HHHHHHHHHHHHHHH	23.70	29472430
446	Phosphorylation	EATETALTCLVEKMN HHHHHHHHHHHHHHC	11.00	22324799
447	S-nitrosocysteine	ATETALTCLVEKMNV HHHHHHHHHHHHHCC	4.10	-
447	Glutathionylation	ATETALTCLVEKMNV HHHHHHHHHHHHHCC	4.10	24333276
447	S-nitrosylation	ATETALTCLVEKMNV HHHHHHHHHHHHHCC	4.10	24895380
447	S-palmitoylation	ATETALTCLVEKMNV HHHHHHHHHHHHHCC	4.10	28526873
460	Acetylation	NVFDTELKGLSKIER CCCCHHHCCCHHHHH	52.12	23954790
460	Ubiquitination	NVFDTELKGLSKIER CCCCHHHCCCHHHHH	52.12	-
464	Malonylation	TELKGLSKIERANAC HHHCCCHHHHHHHHH	54.34	26320211
471	S-nitrosocysteine	KIERANACNSVIKQL HHHHHHHHHHHHHHH	3.80	-
471	Glutathionylation	KIERANACNSVIKQL HHHHHHHHHHHHHHH	3.80	24333276
471	S-nitrosylation	KIERANACNSVIKQL HHHHHHHHHHHHHHH	3.80	20925432
471	S-palmitoylation	KIERANACNSVIKQL HHHHHHHHHHHHHHH	3.80	28526873
476	Acetylation	NACNSVIKQLMKKEF HHHHHHHHHHHCCCC	34.91	22826441
476	Ubiquitination	NACNSVIKQLMKKEF HHHHHHHHHHHCCCC	34.91	-
481	Ubiquitination	VIKQLMKKEFTLEFS HHHHHHCCCCEEEEE	44.06	-
484	Phosphorylation	QLMKKEFTLEFSRDR HHHCCCCEEEEECCC	26.86	24899341
488	Phosphorylation	KEFTLEFSRDRKSMS CCCEEEEECCCCCEE	24.72	23737553
492	Ubiquitination	LEFSRDRKSMSVYCT EEEECCCCCEEEEEC	55.59	-
493	Phosphorylation	EFSRDRKSMSVYCTP EEECCCCCEEEEECC	19.72	27149854
495	Phosphorylation	SRDRKSMSVYCTPNK ECCCCCEEEEECCCC	19.61	27149854
497	Phosphorylation	DRKSMSVYCTPNKPS CCCCEEEEECCCCCC	5.36	29472430
498	S-nitrosocysteine	RKSMSVYCTPNKPSR CCCEEEEECCCCCCC	4.83	-
498	Glutathionylation	RKSMSVYCTPNKPSR CCCEEEEECCCCCCC	4.83	24333276
498	S-nitrosylation	RKSMSVYCTPNKPSR CCCEEEEECCCCCCC	4.83	21278135
498	S-palmitoylation	RKSMSVYCTPNKPSR CCCEEEEECCCCCCC	4.83	28526873
499	Phosphorylation	KSMSVYCTPNKPSRT CCEEEEECCCCCCCC	16.53	29472430
502	Malonylation	SVYCTPNKPSRTSMS EEEECCCCCCCCCHH	45.64	26320211
502	Ubiquitination	SVYCTPNKPSRTSMS EEEECCCCCCCCCHH	45.64	-
504	Phosphorylation	YCTPNKPSRTSMSKM EECCCCCCCCCHHHH	50.21	22817900
506	Phosphorylation	TPNKPSRTSMSKMFV CCCCCCCCCHHHHHC	32.87	27149854
507	Phosphorylation	PNKPSRTSMSKMFVK CCCCCCCCHHHHHCC	21.68	27149854
509	Phosphorylation	KPSRTSMSKMFVKGA CCCCCCHHHHHCCCC	22.27	27149854
510	Ubiquitination	PSRTSMSKMFVKGAP CCCCCHHHHHCCCCC	27.93	-
514	Acetylation	SMSKMFVKGAPEGVI CHHHHHCCCCCCCCC	37.78	22826441
514	Ubiquitination	SMSKMFVKGAPEGVI CHHHHHCCCCCCCCC	37.78	-
524	S-nitrosocysteine	PEGVIDRCTHIRVGS CCCCCCCCCEEEECC	2.62	-
524	Glutathionylation	PEGVIDRCTHIRVGS CCCCCCCCCEEEECC	2.62	24333276
524	S-nitrosylation	PEGVIDRCTHIRVGS CCCCCCCCCEEEECC	2.62	21278135
531	Phosphorylation	CTHIRVGSTKVPMTP CCEEEECCCCCCCCC	23.38	22817900
532	Phosphorylation	THIRVGSTKVPMTPG CEEEECCCCCCCCCC	30.08	29176673
537	Phosphorylation	GSTKVPMTPGVKQKI CCCCCCCCCCHHHHH	15.72	25159016
541	Ubiquitination	VPMTPGVKQKIMSVI CCCCCCHHHHHHHHH	52.36	-
543	Ubiquitination	MTPGVKQKIMSVIRE CCCCHHHHHHHHHHH	34.36	-
546	Phosphorylation	GVKQKIMSVIREWGS CHHHHHHHHHHHHCC	20.19	23737553
553	Phosphorylation	SVIREWGSGSDTLRC HHHHHHCCCHHHHHH	35.88	23737553
555	Phosphorylation	IREWGSGSDTLRCLA HHHHCCCHHHHHHHH	29.17	23737553
557	Phosphorylation	EWGSGSDTLRCLALA HHCCCHHHHHHHHHH	20.14	27742792
560	S-nitrosocysteine	SGSDTLRCLALATHD CCHHHHHHHHHHCCC	2.68	-
560	S-nitrosylation	SGSDTLRCLALATHD CCHHHHHHHHHHCCC	2.68	22178444
565	Phosphorylation	LRCLALATHDNPLKR HHHHHHHCCCCCCCH	30.52	23882026
571	Ubiquitination	ATHDNPLKREEMHLE HCCCCCCCHHHCCHH	60.05	-
580	Phosphorylation	EEMHLEDSANFIKYE HHCCHHHHCCCEEEE	18.75	28066266
608	Phosphorylation	PPRIEVASSVKLCRQ CCCCCHHHHHHHHHH	40.62	23737553
609	Phosphorylation	PRIEVASSVKLCRQA CCCCHHHHHHHHHHC	17.34	23737553
611	Ubiquitination	IEVASSVKLCRQAGI CCHHHHHHHHHHCCC	43.76	-
624	Phosphorylation	GIRVIMITGDNKGTA CCEEEEEECCCCCHH	22.54	28542873
628	Ubiquitination	IMITGDNKGTAVAIC EEEECCCCCHHHHHH	63.48	-
635	S-nitrosocysteine	KGTAVAICRRIGIFG CCHHHHHHHHCCCCC	1.40	-
635	S-nitrosylation	KGTAVAICRRIGIFG CCHHHHHHHHCCCCC	1.40	21278135
648	Phosphorylation	FGQDEDVTSKAFTGR CCCCCCCCCCCCCCC	36.51	23737553
649	Phosphorylation	GQDEDVTSKAFTGRE CCCCCCCCCCCCCCC	23.10	23737553
650	Ubiquitination	QDEDVTSKAFTGREF CCCCCCCCCCCCCCH	37.85	-
653	Phosphorylation	DVTSKAFTGREFDEL CCCCCCCCCCCHHHC	39.94	24925903
661	Phosphorylation	GREFDELSPSAQRDA CCCHHHCCHHHHHHH	18.11	25521595
663	Phosphorylation	EFDELSPSAQRDACL CHHHCCHHHHHHHHH	33.39	24925903
669	S-nitrosocysteine	PSAQRDACLNARCFA HHHHHHHHHHCHHHE	3.36	-
669	Glutathionylation	PSAQRDACLNARCFA HHHHHHHHHHCHHHE	3.36	24333276
669	S-nitrosylation	PSAQRDACLNARCFA HHHHHHHHHHCHHHE	3.36	21278135
712	Ubiquitination	NDAPALKKSEIGIAM CCCCCCCHHHHEEEE	54.92	-
713	Phosphorylation	DAPALKKSEIGIAMG CCCCCCHHHHEEEEC	32.62	25367039
721	Phosphorylation	EIGIAMGSGTAVAKT HHEEEECCCHHHHHC	21.64	27742792
723	Phosphorylation	GIAMGSGTAVAKTAS EEEECCCHHHHHCHH	21.47	25367039
728	Phosphorylation	SGTAVAKTASEMVLA CCHHHHHCHHHHHCC	26.19	25367039
730	Phosphorylation	TAVAKTASEMVLADD HHHHHCHHHHHCCCC	31.30	25367039
740	Phosphorylation	VLADDNFSTIVAAVE HCCCCCCHHHHHHHH	24.39	24719451
741	Phosphorylation	LADDNFSTIVAAVEE CCCCCCHHHHHHHHH	18.48	25367039
757	Ubiquitination	RAIYNNMKQFIRYLI HHHHHCHHHHHHHHH	44.15	-
875	S-palmitoylation	QLSHFLQCKEDNPDF EHHHHHHCCCCCCCC	5.92	28526873
990	Phosphorylation	LKFVARNYLEQPGKE HHHHHHHHHCCCCCC	13.18	22817900
996	Ubiquitination	NYLEQPGKECVQPAT HHHCCCCCCCCCCCC	55.41	-
998	S-nitrosocysteine	LEQPGKECVQPATKS HCCCCCCCCCCCCCC	3.82	-
998	Glutathionylation	LEQPGKECVQPATKS HCCCCCCCCCCCCCC	3.82	24333276
998	S-nitrosylation	LEQPGKECVQPATKS HCCCCCCCCCCCCCC	3.82	22178444
998	S-palmitoylation	LEQPGKECVQPATKS HCCCCCCCCCCCCCC	3.82	26165157

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 AT2A2_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of AT2A2_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 AT2A2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PPLA_MOUSE	Pln	physical	15201433
ATPA_HUMAN	ATP5A1	physical	26496610
ATPB_HUMAN	ATP5B	physical	26496610
AT5F1_HUMAN	ATP5F1	physical	26496610
ATPO_HUMAN	ATP5O	physical	26496610
CLCN7_HUMAN	CLCN7	physical	26496610
DHCR7_HUMAN	DHCR7	physical	26496610
DHC24_HUMAN	DHCR24	physical	26496610
STT3A_HUMAN	STT3A	physical	26496610
PHB_HUMAN	PHB	physical	26496610
PON2_HUMAN	PON2	physical	26496610
ABCD3_HUMAN	ABCD3	physical	26496610
AAAT_HUMAN	SLC1A5	physical	26496610
TAP2_HUMAN	TAP2	physical	26496610
SC22B_HUMAN	SEC22B	physical	26496610
PTSS1_HUMAN	PTDSS1	physical	26496610
VTI1B_HUMAN	VTI1B	physical	26496610
DPOLQ_HUMAN	POLQ	physical	26496610
PHB2_HUMAN	PHB2	physical	26496610
S43A3_HUMAN	SLC43A3	physical	26496610
TMCO1_HUMAN	TMCO1	physical	26496610
T161A_HUMAN	TMEM161A	physical	26496610
OCAD1_HUMAN	OCIAD1	physical	26496610
S35F6_HUMAN	SLC35F6	physical	26496610
TMM33_HUMAN	TMEM33	physical	26496610
ESYT2_HUMAN	ESYT2	physical	26496610
INT2_HUMAN	INTS2	physical	26496610
ALG8_HUMAN	ALG8	physical	26496610
S35E1_HUMAN	SLC35E1	physical	26496610
YIPF5_HUMAN	YIPF5	physical	26496610
T120A_HUMAN	TMEM120A	physical	26496610
RABL3_HUMAN	RABL3	physical	26496610

Drug and Disease Associations

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

Regulatory Network of AT2A2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-663, AND MASSSPECTROMETRY.	17114649 [Abstract]
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-537, AND MASSSPECTROMETRY.	17203969 [Abstract]
Ubiquitylation
Reference	PubMed
"A proteomics approach to identify the ubiquitinated proteins in mouseheart."; Jeon H.B., Choi E.S., Yoon J.H., Hwang J.H., Chang J.W., Lee E.K.,Choi H.W., Park Z.-Y., Yoo Y.J.; Biochem. Biophys. Res. Commun. 357:731-736(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-143, AND MASSSPECTROMETRY.	17451654 [Abstract]