dbPTM

AT2A2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AT2A2_HUMAN
UniProt AC	P16615
Protein Name	Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
Gene Name	ATP2A2
Organism	Homo sapiens (Human).
Sequence Length	1042
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 2 is involved in the regulation of the contraction/relaxation cycle. [PubMed: 16402920 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 (By similarity]
Protein Sequence	MENAHTKTVEEVLGHFGVNESTGLSLEQVKKLKERWGSNELPAEEGKTLLELVIEQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILVANAIVGVWQERNAENAIEALKEYEPEMGKVYRQDRKSVQRIKAKDIVPGDIVEIAVGDKVPADIRLTSIKSTTLRVDQSILTGESVSVIKHTDPVPDPRAVNQDKKNMLFSGTNIAAGKAMGVVVATGVNTEIGKIRDEMVATEQERTPLQQKLDEFGEQLSKVISLICIAVWIINIGHFNDPVHGGSWIRGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFILDRVEGDTCSLNEFTITGSTYAPIGEVHKDDKPVNCHQYDGLVELATICALCNDSALDYNEAKGVYEKVGEATETALTCLVEKMNVFDTELKGLSKIERANACNSVIKQLMKKEFTLEFSRDRKSMSVYCTPNKPSRTSMSKMFVKGAPEGVIDRCTHIRVGSTKVPMTSGVKQKIMSVIREWGSGSDTLRCLALATHDNPLRREEMHLEDSANFIKYETNLTFVGCVGMLDPPRIEVASSVKLCRQAGIRVIMITGDNKGTAVAICRRIGIFGQDEDVTSKAFTGREFDELNPSAQRDACLNARCFARVEPSHKSKIVEFLQSFDEITAMTGDGVNDAPALKKAEIGIAMGSGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVCIFLTAALGFPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMNKPPRNPKEPLISGWLFFRYLAIGCYVGAATVGAAAWWFIAADGGPRVSFYQLSHFLQCKEDNPDFEGVDCAIFESPYPMTMALSVLVTIEMCNALNSLSENQSLLRMPPWENIWLVGSICLSMSLHFLILYVEPLPLIFQITPLNVTQWLMVLKISLPVILMDETLKFVARNYLEPGKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
30	2-Hydroxyisobutyrylation	GLSLEQVKKLKERWG CCCHHHHHHHHHHHC	52.67	-
30	Ubiquitination	GLSLEQVKKLKERWG CCCHHHHHHHHHHHC	52.67	21906983
30 (in isoform 1)	Ubiquitination	-	52.67	21890473
30 (in isoform 2)	Ubiquitination	-	52.67	21890473
31	Acetylation	LSLEQVKKLKERWGS CCHHHHHHHHHHHCC	66.97	18530349
31	Ubiquitination	LSLEQVKKLKERWGS CCHHHHHHHHHHHCC	66.97	-
33	Acetylation	LEQVKKLKERWGSNE HHHHHHHHHHHCCCC	54.86	18530359
38	Phosphorylation	KLKERWGSNELPAEE HHHHHHCCCCCCHHH	21.85	21815630
120	Ubiquitination	ENAIEALKEYEPEMG HHHHHHHHHHCHHHC	66.36	21906983
120 (in isoform 1)	Ubiquitination	-	66.36	21890473
120 (in isoform 2)	Ubiquitination	-	66.36	21890473
122	Nitration	AIEALKEYEPEMGKV HHHHHHHHCHHHCCH	34.89	-
122	Phosphorylation	AIEALKEYEPEMGKV HHHHHHHHCHHHCCH	34.89	18083107
128	2-Hydroxyisobutyrylation	EYEPEMGKVYRQDRK HHCHHHCCHHHCCHH	34.48	-
128	Ubiquitination	EYEPEMGKVYRQDRK HHCHHHCCHHHCCHH	34.48	-
128 (in isoform 1)	Ubiquitination	-	34.48	21890473
128 (in isoform 2)	Ubiquitination	-	34.48	21890473
130	Nitration	EPEMGKVYRQDRKSV CHHHCCHHHCCHHHH	13.17	-
135	Glycation	KVYRQDRKSVQRIKA CHHHCCHHHHHHHHH	64.37	-
141	Glycation	RKSVQRIKAKDIVPG HHHHHHHHHHHCCCC	52.12	-
143	2-Hydroxyisobutyrylation	SVQRIKAKDIVPGDI HHHHHHHHHCCCCCE	42.88	-
143	Ubiquitination	SVQRIKAKDIVPGDI HHHHHHHHHCCCCCE	42.88	-
143 (in isoform 2)	Ubiquitination	-	42.88	-
158	2-Hydroxyisobutyrylation	VEIAVGDKVPADIRL EEEECCCCCCCCEEE	44.16	-
158	Ubiquitination	VEIAVGDKVPADIRL EEEECCCCCCCCEEE	44.16	-
158 (in isoform 2)	Ubiquitination	-	44.16	-
164	Methylation	DKVPADIRLTSIKST CCCCCCEEEEECCCC	32.25	115916465
169	Malonylation	DIRLTSIKSTTLRVD CEEEEECCCCEEEEE	41.33	26320211
169	Ubiquitination	DIRLTSIKSTTLRVD CEEEEECCCCEEEEE	41.33	21906983
169 (in isoform 1)	Ubiquitination	-	41.33	21890473
169 (in isoform 2)	Ubiquitination	-	41.33	21890473
170	Phosphorylation	IRLTSIKSTTLRVDQ EEEEECCCCEEEEEC	25.59	24719451
178	Ubiquitination	TTLRVDQSILTGESV CEEEEECHHHCCCCE	18.33	21890473
178	Phosphorylation	TTLRVDQSILTGESV CEEEEECHHHCCCCE	18.33	20068231
181	Phosphorylation	RVDQSILTGESVSVI EEECHHHCCCCEEEE	36.91	30266825
184	Phosphorylation	QSILTGESVSVIKHT CHHHCCCCEEEEECC	22.49	30266825
186	Phosphorylation	ILTGESVSVIKHTDP HHCCCCEEEEECCCC	27.66	30266825
189	2-Hydroxyisobutyrylation	GESVSVIKHTDPVPD CCCEEEEECCCCCCC	37.99	-
189	Acetylation	GESVSVIKHTDPVPD CCCEEEEECCCCCCC	37.99	26051181
189	Ubiquitination	GESVSVIKHTDPVPD CCCEEEEECCCCCCC	37.99	-
189 (in isoform 2)	Ubiquitination	-	37.99	-
191	Phosphorylation	SVSVIKHTDPVPDPR CEEEEECCCCCCCCC	36.68	22210691
205	Ubiquitination	RAVNQDKKNMLFSGT CCCCCCCCCCCCCCC	56.74	21890473
205	Malonylation	RAVNQDKKNMLFSGT CCCCCCCCCCCCCCC	56.74	26320211
205	Ubiquitination	RAVNQDKKNMLFSGT CCCCCCCCCCCCCCC	56.74	21890473
205 (in isoform 1)	Ubiquitination	-	56.74	21890473
205 (in isoform 2)	Ubiquitination	-	56.74	21890473
218	Acetylation	GTNIAAGKAMGVVVA CCCCCCCCCCEEEEE	30.39	7364683
226	Phosphorylation	AMGVVVATGVNTEIG CCEEEEEECCCCCCH	30.01	21406692
230	Phosphorylation	VVATGVNTEIGKIRD EEEECCCCCCHHHHH	26.94	21406692
239	Sulfoxidation	IGKIRDEMVATEQER CHHHHHHHHCCHHHC	2.66	21406390
242	Phosphorylation	IRDEMVATEQERTPL HHHHHHCCHHHCCHH	27.13	-
247	Phosphorylation	VATEQERTPLQQKLD HCCHHHCCHHHHHHH	27.83	23879269
252	Ubiquitination	ERTPLQQKLDEFGEQ HCCHHHHHHHHHHHH	44.97	21906983
252 (in isoform 1)	Ubiquitination	-	44.97	21890473
252 (in isoform 2)	Ubiquitination	-	44.97	21890473
261	Phosphorylation	DEFGEQLSKVISLIC HHHHHHHHHHHHHHH	25.27	21406692
268	Glutathionylation	SKVISLICIAVWIIN HHHHHHHHHHHHHHH	1.66	15489859
294	Nitrated tyrosine	SWIRGAIYYFKIAVA CCHHHHHHHHHHHHH	11.43	-
294	Nitration	SWIRGAIYYFKIAVA CCHHHHHHHHHHHHH	11.43	16399855
294	Nitration	SWIRGAIYYFKIAVA CCHHHHHHHHHHHHH	11.43	16399855
294	Phosphorylation	SWIRGAIYYFKIAVA CCHHHHHHHHHHHHH	11.43	-
295	Nitrated tyrosine	WIRGAIYYFKIAVAL CHHHHHHHHHHHHHH	7.71	-
295	Nitration	WIRGAIYYFKIAVAL CHHHHHHHHHHHHHH	7.71	16399855
295	Nitration	WIRGAIYYFKIAVAL CHHHHHHHHHHHHHH	7.71	16399855
328	Ubiquitination	LGTRRMAKKNAIVRS HCCHHHHHHCHHHHC	36.90	-
329	Ubiquitination	GTRRMAKKNAIVRSL CCHHHHHHCHHHHCC	41.91	-
335	Phosphorylation	KKNAIVRSLPSVETL HHCHHHHCCCCCCCC	33.46	22210691
338	Phosphorylation	AIVRSLPSVETLGCT HHHHCCCCCCCCCCC	37.57	26437602
341	Phosphorylation	RSLPSVETLGCTSVI HCCCCCCCCCCCEEE	26.71	22210691
345	Phosphorylation	SVETLGCTSVICSDK CCCCCCCCEEEEECC	24.99	28348404
346	Phosphorylation	VETLGCTSVICSDKT CCCCCCCEEEEECCC	17.35	26437602
350	Phosphorylation	GCTSVICSDKTGTLT CCCEEEEECCCCCCC	30.90	28348404
352	Ubiquitination	TSVICSDKTGTLTTN CEEEEECCCCCCCCC	32.34	-
353	Phosphorylation	SVICSDKTGTLTTNQ EEEEECCCCCCCCCC	40.15	24719451
357	Phosphorylation	SDKTGTLTTNQMSVC ECCCCCCCCCCCCHH	24.44	24719451
358	Phosphorylation	DKTGTLTTNQMSVCR CCCCCCCCCCCCHHE	26.94	22210691
361	Sulfoxidation	GTLTTNQMSVCRMFI CCCCCCCCCHHEEEE	3.35	21406390
362	Phosphorylation	TLTTNQMSVCRMFIL CCCCCCCCHHEEEEE	14.32	26437602
376	Phosphorylation	LDRVEGDTCSLNEFT EEECCCCCCCCEEEE	18.17	25850435
378	Phosphorylation	RVEGDTCSLNEFTIT ECCCCCCCCEEEEEE	36.00	25849741
383	Phosphorylation	TCSLNEFTITGSTYA CCCCEEEEEECCEEE	16.08	25850435
385	Phosphorylation	SLNEFTITGSTYAPI CCEEEEEECCEEECC	23.25	25850435
400	Ubiquitination	GEVHKDDKPVNCHQY CEECCCCCCCCCCCC	62.08	-
427	Phosphorylation	CNDSALDYNEAKGVY HCCCCCCHHHHCCHH	18.76	-
431	Ubiquitination	ALDYNEAKGVYEKVG CCCHHHHCCHHHHHH	42.61	-
433	Ubiquitination	DYNEAKGVYEKVGEA CHHHHCCHHHHHHHH	5.71	21890473
436	2-Hydroxyisobutyrylation	EAKGVYEKVGEATET HHCCHHHHHHHHHHH	37.54	-
436	Ubiquitination	EAKGVYEKVGEATET HHCCHHHHHHHHHHH	37.54	-
441	Phosphorylation	YEKVGEATETALTCL HHHHHHHHHHHHHHH	29.57	29255136
443	Phosphorylation	KVGEATETALTCLVE HHHHHHHHHHHHHHH	23.70	29255136
446	Phosphorylation	EATETALTCLVEKMN HHHHHHHHHHHHHHC	11.00	20860994
447	Glutathionylation	ATETALTCLVEKMNV HHHHHHHHHHHHHCC	4.10	22555962
451	Acetylation	ALTCLVEKMNVFDTE HHHHHHHHHCCCCHH	28.44	26051181
451	Ubiquitination	ALTCLVEKMNVFDTE HHHHHHHHHCCCCHH	28.44	-
460	Ubiquitination	NVFDTELKGLSKIER CCCCHHHCCCHHHHH	52.12	21890473
460	2-Hydroxyisobutyrylation	NVFDTELKGLSKIER CCCCHHHCCCHHHHH	52.12	-
460	Acetylation	NVFDTELKGLSKIER CCCCHHHCCCHHHHH	52.12	25953088
460	Glycation	NVFDTELKGLSKIER CCCCHHHCCCHHHHH	52.12	-
460	Ubiquitination	NVFDTELKGLSKIER CCCCHHHCCCHHHHH	52.12	21890473
460 (in isoform 1)	Ubiquitination	-	52.12	21890473
460 (in isoform 2)	Ubiquitination	-	52.12	21890473
464	Acetylation	TELKGLSKIERANAC HHHCCCHHHHHHHHH	54.34	23749302
464	Malonylation	TELKGLSKIERANAC HHHCCCHHHHHHHHH	54.34	26320211
464	Ubiquitination	TELKGLSKIERANAC HHHCCCHHHHHHHHH	54.34	19608861
473	Phosphorylation	ERANACNSVIKQLMK HHHHHHHHHHHHHHC	25.71	26437602
476	2-Hydroxyisobutyrylation	NACNSVIKQLMKKEF HHHHHHHHHHHCCCC	34.91	-
476	Acetylation	NACNSVIKQLMKKEF HHHHHHHHHHHCCCC	34.91	25825284
476	Glycation	NACNSVIKQLMKKEF HHHHHHHHHHHCCCC	34.91	-
476	Ubiquitination	NACNSVIKQLMKKEF HHHHHHHHHHHCCCC	34.91	-
480	Sumoylation	SVIKQLMKKEFTLEF HHHHHHHCCCCEEEE	58.71	-
480	Sumoylation	SVIKQLMKKEFTLEF HHHHHHHCCCCEEEE	58.71	-
481	2-Hydroxyisobutyrylation	VIKQLMKKEFTLEFS HHHHHHCCCCEEEEE	44.06	-
481	Acetylation	VIKQLMKKEFTLEFS HHHHHHCCCCEEEEE	44.06	54417127
481	Glycation	VIKQLMKKEFTLEFS HHHHHHCCCCEEEEE	44.06	-
481	Ubiquitination	VIKQLMKKEFTLEFS HHHHHHCCCCEEEEE	44.06	-
484	Phosphorylation	QLMKKEFTLEFSRDR HHHCCCCEEEEECCC	26.86	22673903
488	Phosphorylation	KEFTLEFSRDRKSMS CCCEEEEECCCCCEE	24.72	21712546
492	2-Hydroxyisobutyrylation	LEFSRDRKSMSVYCT EEEECCCCCEEEEEC	55.59	-
492	Malonylation	LEFSRDRKSMSVYCT EEEECCCCCEEEEEC	55.59	26320211
492	Ubiquitination	LEFSRDRKSMSVYCT EEEECCCCCEEEEEC	55.59	-
493	Phosphorylation	EFSRDRKSMSVYCTP EEECCCCCEEEEECC	19.72	27080861
495	Phosphorylation	SRDRKSMSVYCTPNK ECCCCCEEEEECCCC	19.61	27080861
497	Nitration	DRKSMSVYCTPNKPS CCCCEEEEECCCCCC	5.36	-
497	Phosphorylation	DRKSMSVYCTPNKPS CCCCEEEEECCCCCC	5.36	29214152
498	Glutathionylation	RKSMSVYCTPNKPSR CCCEEEEECCCCCCC	4.83	22555962
498	S-nitrosylation	RKSMSVYCTPNKPSR CCCEEEEECCCCCCC	4.83	24105792
499	Phosphorylation	KSMSVYCTPNKPSRT CCEEEEECCCCCCCC	16.53	25159151
502	Acetylation	SVYCTPNKPSRTSMS EEEECCCCCCCCCHH	45.64	26051181
502	Ubiquitination	SVYCTPNKPSRTSMS EEEECCCCCCCCCHH	45.64	-
504	Phosphorylation	YCTPNKPSRTSMSKM EECCCCCCCCCHHHH	50.21	26437602
507	Phosphorylation	PNKPSRTSMSKMFVK CCCCCCCCHHHHHCC	21.68	26437602
510	Acetylation	PSRTSMSKMFVKGAP CCCCCHHHHHCCCCC	27.93	25953088
510	Malonylation	PSRTSMSKMFVKGAP CCCCCHHHHHCCCCC	27.93	26320211
510	Ubiquitination	PSRTSMSKMFVKGAP CCCCCHHHHHCCCCC	27.93	-
514	2-Hydroxyisobutyrylation	SMSKMFVKGAPEGVI CHHHHHCCCCCCCCC	37.78	-
514	Acetylation	SMSKMFVKGAPEGVI CHHHHHCCCCCCCCC	37.78	26051181
514	Malonylation	SMSKMFVKGAPEGVI CHHHHHCCCCCCCCC	37.78	26320211
514	Ubiquitination	SMSKMFVKGAPEGVI CHHHHHCCCCCCCCC	37.78	21906983
514 (in isoform 1)	Ubiquitination	-	37.78	21890473
514 (in isoform 2)	Ubiquitination	-	37.78	21890473
523	Methylation	APEGVIDRCTHIRVG CCCCCCCCCCEEEEC	18.99	115916469
524	Glutathionylation	PEGVIDRCTHIRVGS CCCCCCCCCEEEECC	2.62	15489859
525	Phosphorylation	EGVIDRCTHIRVGST CCCCCCCCEEEECCC	22.64	26437602
531	Phosphorylation	CTHIRVGSTKVPMTS CCEEEECCCCCCCCH	23.38	30108239
532	Phosphorylation	THIRVGSTKVPMTSG CEEEECCCCCCCCHH	30.08	30108239
533	Ubiquitination	HIRVGSTKVPMTSGV EEEECCCCCCCCHHH	46.14	21906983
533 (in isoform 1)	Ubiquitination	-	46.14	21890473
533 (in isoform 2)	Ubiquitination	-	46.14	21890473
537	Phosphorylation	GSTKVPMTSGVKQKI CCCCCCCCHHHHHHH	19.09	26437602
538	Phosphorylation	STKVPMTSGVKQKIM CCCCCCCHHHHHHHH	35.02	26437602
541	2-Hydroxyisobutyrylation	VPMTSGVKQKIMSVI CCCCHHHHHHHHHHH	49.77	-
541	Acetylation	VPMTSGVKQKIMSVI CCCCHHHHHHHHHHH	49.77	25953088
541	Ubiquitination	VPMTSGVKQKIMSVI CCCCHHHHHHHHHHH	49.77	21906983
541 (in isoform 1)	Ubiquitination	-	49.77	21890473
541 (in isoform 2)	Ubiquitination	-	49.77	21890473
543	Ubiquitination	MTSGVKQKIMSVIRE CCHHHHHHHHHHHHH	34.36	-
546	Phosphorylation	GVKQKIMSVIREWGS HHHHHHHHHHHHHCC	20.19	29083192
549	Methylation	QKIMSVIREWGSGSD HHHHHHHHHHCCCHH	31.31	115916473
553	Phosphorylation	SVIREWGSGSDTLRC HHHHHHCCCHHHHHH	35.88	29083192
555	Phosphorylation	IREWGSGSDTLRCLA HHHHCCCHHHHHHHH	29.17	29083192
557	Phosphorylation	EWGSGSDTLRCLALA HHCCCHHHHHHHHHH	20.14	29083192
560	S-nitrosocysteine	SGSDTLRCLALATHD CCHHHHHHHHHHCCC	2.68	-
560	Glutathionylation	SGSDTLRCLALATHD CCHHHHHHHHHHCCC	2.68	15489859
560	S-nitrosylation	SGSDTLRCLALATHD CCHHHHHHHHHHCCC	2.68	20140087
575	Sulfoxidation	NPLRREEMHLEDSAN CCCHHHHCCHHHHCC	3.61	21406390
580	Phosphorylation	EEMHLEDSANFIKYE HHCCHHHHCCCEEEE	18.75	26471730
585	Sumoylation	EDSANFIKYETNLTF HHHCCCEEEECCCEE	32.66	-
585	Sumoylation	EDSANFIKYETNLTF HHHCCCEEEECCCEE	32.66	-
586	Nitration	DSANFIKYETNLTFV HHCCCEEEECCCEEE	24.14	-
608	Phosphorylation	PPRIEVASSVKLCRQ CCCCCHHHHHHHHHH	40.62	29255136
609	Phosphorylation	PRIEVASSVKLCRQA CCCCHHHHHHHHHHC	17.34	29255136
611	Acetylation	IEVASSVKLCRQAGI CCHHHHHHHHHHCCC	43.76	26051181
611	Ubiquitination	IEVASSVKLCRQAGI CCHHHHHHHHHHCCC	43.76	22053931
611 (in isoform 1)	Ubiquitination	-	43.76	21890473
611 (in isoform 2)	Ubiquitination	-	43.76	21890473
613	Glutathionylation	VASSVKLCRQAGIRV HHHHHHHHHHCCCEE	2.22	15489859
623	Ubiquitination	AGIRVIMITGDNKGT CCCEEEEEECCCCCH	2.40	21890473
624	Phosphorylation	GIRVIMITGDNKGTA CCEEEEEECCCCCHH	22.54	21406692
628	Ubiquitination	IMITGDNKGTAVAIC EEEECCCCCHHHHHH	63.48	-
648	Phosphorylation	FGQDEDVTSKAFTGR CCCCCCCCCCCCCCC	36.51	22673903
649	Phosphorylation	GQDEDVTSKAFTGRE CCCCCCCCCCCCCCC	23.10	22673903
650	Ubiquitination	QDEDVTSKAFTGREF CCCCCCCCCCCCCCH	37.85	21890473
650	Acetylation	QDEDVTSKAFTGREF CCCCCCCCCCCCCCH	37.85	25953088
650	Ubiquitination	QDEDVTSKAFTGREF CCCCCCCCCCCCCCH	37.85	21890473
650 (in isoform 1)	Ubiquitination	-	37.85	21890473
650 (in isoform 2)	Ubiquitination	-	37.85	21890473
653	Phosphorylation	DVTSKAFTGREFDEL CCCCCCCCCCCHHHC	39.94	23403867
663	Phosphorylation	EFDELNPSAQRDACL CHHHCCHHHHHHHHH	35.64	19664994
669	Glutathionylation	PSAQRDACLNARCFA HHHHHHHHHHHHHHE	3.36	15489859
674	Glutathionylation	DACLNARCFARVEPS HHHHHHHHHEECCCC	2.65	22833525
683	Glycation	ARVEPSHKSKIVEFL EECCCCCHHHHHHHH	58.75	-
683	Ubiquitination	ARVEPSHKSKIVEFL EECCCCCHHHHHHHH	58.75	-
685	Ubiquitination	VEPSHKSKIVEFLQS CCCCCHHHHHHHHHC	56.42	-
685 (in isoform 2)	Ubiquitination	-	56.42	-
692	Phosphorylation	KIVEFLQSFDEITAM HHHHHHHCCHHHHCC	36.49	22673903
697	Phosphorylation	LQSFDEITAMTGDGV HHCCHHHHCCCCCCC	14.34	22673903
699	Sulfoxidation	SFDEITAMTGDGVND CCHHHHCCCCCCCCC	3.01	28183972
711	Ubiquitination	VNDAPALKKAEIGIA CCCCHHHHHCCCEEE	52.63	21906983
711 (in isoform 1)	Ubiquitination	-	52.63	21890473
711 (in isoform 2)	Ubiquitination	-	52.63	21890473
712	Ubiquitination	NDAPALKKAEIGIAM CCCHHHHHCCCEEEE	52.69	-
712 (in isoform 1)	Ubiquitination	-	52.69	21890473
712 (in isoform 2)	Ubiquitination	-	52.69	21890473
721	Phosphorylation	EIGIAMGSGTAVAKT CCEEEECCCHHHHHC	21.64	-
723	Phosphorylation	GIAMGSGTAVAKTAS EEEECCCHHHHHCHH	21.47	30278072
728	Phosphorylation	SGTAVAKTASEMVLA CCHHHHHCHHHHHCC	26.19	30278072
730	Ubiquitination	TAVAKTASEMVLADD HHHHHCHHHHHCCCC	31.30	21890473
730	Phosphorylation	TAVAKTASEMVLADD HHHHHCHHHHHCCCC	31.30	30278072
732	Sulfoxidation	VAKTASEMVLADDNF HHHCHHHHHCCCCCC	2.51	28183972
740	Phosphorylation	VLADDNFSTIVAAVE HCCCCCCHHHHHHHH	24.39	24719451
741	Phosphorylation	LADDNFSTIVAAVEE CCCCCCHHHHHHHHH	18.48	-
753	Nitration	VEEGRAIYNNMKQFI HHHHHHHHHCHHHHH	10.25	-
757	Ubiquitination	RAIYNNMKQFIRYLI HHHHHCHHHHHHHHH	44.15	21890473
757	2-Hydroxyisobutyrylation	RAIYNNMKQFIRYLI HHHHHCHHHHHHHHH	44.15	-
757	Acetylation	RAIYNNMKQFIRYLI HHHHHCHHHHHHHHH	44.15	24588123
757	Ubiquitination	RAIYNNMKQFIRYLI HHHHHCHHHHHHHHH	44.15	21890473
757 (in isoform 1)	Ubiquitination	-	44.15	21890473
757 (in isoform 2)	Ubiquitination	-	44.15	21890473
824	Ubiquitination	NKPPRNPKEPLISGW CCCCCCCCCCCHHHH	75.43	-
829	Phosphorylation	NPKEPLISGWLFFRY CCCCCCHHHHHHHHH	31.44	27251275
836	Phosphorylation	SGWLFFRYLAIGCYV HHHHHHHHHHHHHHH	8.70	-
867	Phosphorylation	GGPRVSFYQLSHFLQ CCCEEEEEHHHHHHC	10.88	-
920	Phosphorylation	NSLSENQSLLRMPPW HCCCCCCCHHCCCCC	40.74	24719451
973	Phosphorylation	WLMVLKISLPVILMD HHHHHHHCCCCHHCC	25.65	-
982	Phosphorylation	PVILMDETLKFVARN CCHHCCHHHHHHHHH	30.86	-
990	Nitration	LKFVARNYLEPGKEC HHHHHHHCCCCCCCC	13.59	-
990	Phosphorylation	LKFVARNYLEPGKEC HHHHHHHCCCCCCCC	13.59	28152594
995	Acetylation	RNYLEPGKECVQPAT HHCCCCCCCCCCCCC	59.67	26051181
995	Malonylation	RNYLEPGKECVQPAT HHCCCCCCCCCCCCC	59.67	26320211
995	Ubiquitination	RNYLEPGKECVQPAT HHCCCCCCCCCCCCC	59.67	2190698
995 (in isoform 1)	Ubiquitination	-	59.67	21890473
997	Glutathionylation	YLEPGKECVQPATKS CCCCCCCCCCCCCCC	3.82	22555962

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	CAMK2-FAMILY	-	GPS
38	S	Phosphorylation	Kinase	CAMK-FAMILY	-	GPS
38	S	Phosphorylation	Kinase	CAM-KII_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of AT2A2_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PPLA_HUMAN	PLN	physical	11854448
ITPR3_HUMAN	ITPR3	physical	22939629
NDUS4_HUMAN	NDUFS4	physical	26344197
NOTC2_HUMAN	NOTCH2	physical	26344197

Drug and Disease Associations

Kegg Disease
H00715	Darier disease; Dyskeratosis follicularis
H00755	Acrokeratosis verruciformis
OMIM Disease
101900	Acrokeratosis verruciformis (AKV)
124200	Darier disease (DD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of AT2A2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-464, AND MASS SPECTROMETRY.	19608861 [Abstract]
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]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, AND MASSSPECTROMETRY.	19690332 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, AND MASSSPECTROMETRY.	15302935 [Abstract]