dbPTM

AT2A2_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AT2A2_RAT
UniProt AC	P11507
Protein Name	Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
Gene Name	Atp2a2
Organism	Rattus norvegicus (Rat).
Sequence Length	1043
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..
Protein Sequence	MENAHTKTVEEVLGHFGVNESTGLSLEQVKKLKERWGSNELPAEEGKTLLELVIEQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILVANAIVGVWQERNAENAIEALKEYEPEMGKVYRQDRKSVQRIKAKDIVPGDIVEIAVGDKVPADIRLTSIKSTTLRVDQSILTGESVSVIKHTDPVPDPRAVNQDKKNMLFSGTNIAAGKAMGVVVATGVNTEIGKIRDEMVATEQERTPLQQKLDEFGEQLSKVISLICIAVWIINIGHFNDPVHGGSWIRGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFILDKVEGDTCSLNEFTITGSTYAPIGEVQKDDKPVKCHQYDGLVELATICALCNDSALDYNEAKGVYEKVGEATETALTCLVEKMNVFDTELKGLSKIERANACNSVIKQLMKKEFTLEFSRDRKSMSVYCTPNKPSRTSMSKMFVKGAPEGVIDRCTHIRVGSTKVPMTPGVKQKIMSVIREWGSGSDTLRCLALATHDNPLRREEMHLEDSANFIKYETNLTFVGCVGMLDPPRIEVASSVKLCRQAGIRVIMITGDNKGTAVAICRRIGIFGQDEDVTSKAFTGREFDELSPSAQRDACLNARCFARVEPSHKSKIVEFLQSFDEITAMTGDGVNDAPALKKSEIGIAMGSGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVCIFLTAALGFPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMNKPPRNPKEPLISGWLFFRYLAIGCYVGAATVGAAAWWFIAADGGPRVSFYQLSHFLQCKEDNPDFEGVDCAIFESPYPMTMALSVLVTIEMCNALNSLSENQSLLRMPPWENIWLVGSICLSMSLHFLILYVEPLPLIFQITPLNLTQWLMVLKISLPVILMDETLKFVARNYLEPGKECAQPATKPSCSLSACTDGISWPFVLLIMPLVVWVYSTDTNFSDMFWS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
38	Phosphorylation	KLKERWGSNELPAEE HHHHHHCCCCCCHHH	21.85	22817900
128	Acetylation	EYEPEMGKVYRQDRK HHCHHHCCHHHCCHH	34.48	22902405
169	Acetylation	DIRLTSIKSTTLRVD CEEEEECCCCEEEEE	41.33	22902405
186	Phosphorylation	ILTGESVSVIKHTDP HHCCCCEEEEECCCC	27.66	22673903
189	Acetylation	GESVSVIKHTDPVPD CCCEEEEECCCCCCC	37.99	22902405
204	Acetylation	PRAVNQDKKNMLFSG CCCCCCCCCCCCCCC	35.96	22902405
205	Acetylation	RAVNQDKKNMLFSGT CCCCCCCCCCCCCCC	56.74	22902405
210	Phosphorylation	DKKNMLFSGTNIAAG CCCCCCCCCCCCCCC	40.52	22673903
212	Phosphorylation	KNMLFSGTNIAAGKA CCCCCCCCCCCCCCC	23.42	22673903
294	Nitrated tyrosine	SWIRGAIYYFKIAVA CCHHHHHHHHHHHHH	11.43	-
294	Nitration	SWIRGAIYYFKIAVA CCHHHHHHHHHHHHH	11.43	16399855
294	Nitration	SWIRGAIYYFKIAVA CCHHHHHHHHHHHHH	11.43	16399855
295	Nitrated tyrosine	WIRGAIYYFKIAVAL CHHHHHHHHHHHHHH	7.71	-
295	Nitration	WIRGAIYYFKIAVAL CHHHHHHHHHHHHHH	7.71	16399855
295	Nitration	WIRGAIYYFKIAVAL CHHHHHHHHHHHHHH	7.71	16399855
376	Phosphorylation	LDKVEGDTCSLNEFT EEECCCCCEECEEEE	18.17	27097102
378	Phosphorylation	KVEGDTCSLNEFTIT ECCCCCEECEEEEEE	36.00	27097102
383	Phosphorylation	TCSLNEFTITGSTYA CEECEEEEEECCEEE	16.08	27097102
385	Phosphorylation	SLNEFTITGSTYAPI ECEEEEEECCEEEEC	23.25	27097102
407	Phosphorylation	KPVKCHQYDGLVELA CCCCCCCCCCHHHHH	6.57	-
441	Phosphorylation	YEKVGEATETALTCL HHHHHHHHHHHHHHH	29.57	29779826
443	Phosphorylation	KVGEATETALTCLVE HHHHHHHHHHHHHHH	23.70	23984901
446	Phosphorylation	EATETALTCLVEKMN HHHHHHHHHHHHHHC	11.00	23984901
460	Acetylation	NVFDTELKGLSKIER CCCCHHHCCCHHHHH	52.12	22902405
464	Acetylation	TELKGLSKIERANAC HHHCCCHHHHHHHHH	54.34	22902405
484	Phosphorylation	QLMKKEFTLEFSRDR HHHCCCCEEEEECCC	26.86	22673903
488	Phosphorylation	KEFTLEFSRDRKSMS CCCEEEEECCCCCEE	24.72	22673903
497	Phosphorylation	DRKSMSVYCTPNKPS CCCCEEEEECCCCCC	5.36	-
510	Acetylation	PSRTSMSKMFVKGAP CCCCCHHHHHCCCCC	27.93	22902405
514	Acetylation	SMSKMFVKGAPEGVI CHHHHHCCCCCCCCC	37.78	22902405
531	Phosphorylation	CTHIRVGSTKVPMTP CCEEEECCCCCCCCC	23.38	23984901
532	Phosphorylation	THIRVGSTKVPMTPG CEEEECCCCCCCCCC	30.08	23984901
537	Phosphorylation	GSTKVPMTPGVKQKI CCCCCCCCCCHHHHH	15.72	25403869
546	Phosphorylation	GVKQKIMSVIREWGS CHHHHHHHHHHHHCC	20.19	22673903
553	Phosphorylation	SVIREWGSGSDTLRC HHHHHHCCCHHHHHH	35.88	22673903
555	Phosphorylation	IREWGSGSDTLRCLA HHHHCCCHHHHHHHH	29.17	22673903
557	Phosphorylation	EWGSGSDTLRCLALA HHCCCHHHHHHHHHH	20.14	22673903
580	Phosphorylation	EEMHLEDSANFIKYE HHCCHHHHCCCEEEE	18.75	-
608	Phosphorylation	PPRIEVASSVKLCRQ CCCCCHHHHHHHHHH	40.62	22673903
609	Phosphorylation	PRIEVASSVKLCRQA CCCCHHHHHHHHHHC	17.34	22673903
624	Phosphorylation	GIRVIMITGDNKGTA CCEEEEEECCCCCHH	22.54	22673903
648	Phosphorylation	FGQDEDVTSKAFTGR CCCCCCCCCCCCCCC	36.51	22673903
649	Phosphorylation	GQDEDVTSKAFTGRE CCCCCCCCCCCCCCC	23.10	22673903
653	Phosphorylation	DVTSKAFTGREFDEL CCCCCCCCCCCHHHC	39.94	28689409
661	Phosphorylation	GREFDELSPSAQRDA CCCHHHCCHHHHHHH	18.11	27097102
663	Phosphorylation	EFDELSPSAQRDACL CHHHCCHHHHHHHHH	33.39	2844797
867	Phosphorylation	GGPRVSFYQLSHFLQ CCCEEEEEHHHHHHC	10.88	-
876	Acetylation	LSHFLQCKEDNPDFE HHHHHCCCCCCCCCC	55.96	26302492
990	Nitration	LKFVARNYLEPGKEC HHHHHHHCCCCCCCC	13.59	-

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
38	S	Phosphorylation	Kinase	CAMK2A	P11798	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of AT2A2_RAT !!

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_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of AT2A2_RAT !!

Drug and Disease Associations

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

Regulatory Network of AT2A2_RAT

Related Literatures of Post-Translational Modification

Nitration
Reference	PubMed
"Detection of sequence-specific tyrosine nitration of manganese SODand SERCA in cardiovascular disease and aging."; Xu S., Ying J., Jiang B., Guo W., Adachi T., Sharov V., Lazar H.,Menzoian J., Knyushko T.V., Bigelow D., Schoeneich C., Cohen R.A.; Am. J. Physiol. 290:H2220-H2227(2006). Cited for: NITRATION AT TYR-294 AND TYR-295.	16399855 [Abstract]