dbPTM

SAE2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SAE2_HUMAN
UniProt AC	Q9UBT2
Protein Name	SUMO-activating enzyme subunit 2
Gene Name	UBA2
Organism	Homo sapiens (Human).
Sequence Length	640
Subcellular Localization	Cytoplasm. Nucleus. Shuttles between the cytoplasm and the nucleus, sumoylation is required either for nuclear translocation or nuclear retention.
Protein Description	The heterodimer acts as an E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2..
Protein Sequence	MALSRGLPRELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDSIMNPDYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYECHPKPTQRTFPGCTIRNTPSEPIHCIVWAKYLFNQLFGEEDADQEVSPDRADPEAAWEPTEAEARARASNEDGDIKRISTKEWAKSTGYDPVKLFTKLFKDDIRYLLTMDKLWRKRKPPVPLDWAEVQSQGEETNASDQQNEPQLGLKDQQVLDVKSYARLFSKSIETLRVHLAEKGDGAELIWDKDDPSAMDFVTSAANLRMHIFSMNMKSRFDIKSMAGNIIPAIATTNAVIAGLIVLEGLKILSGKIDQCRTIFLNKQPNPRKKLLVPCALDPPNPNCYVCASKPEVTVRLNVHKVTVLTLQDKIVKEKFAMVAPDVQIEDGKGTILISSEEGETEANNHKKLSEFGIRNGSRLQADDFLQDYTLLINILHSEDLGKDVEFEVVGDAPEKVGPKQAEDAAKSITNGSDDGAQPSTSTAQEQDDVLIVDSDEEDSSNNADVSEEERSRKRKLDEKENLSAKRSRIEQKEELDDVIALD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
57	Ubiquitination	DTIDVSNLNRQFLFQ CCCCHHHCCHHHHHC	4.32	-
65	Ubiquitination	NRQFLFQKKHVGRSK CHHHHHCCCCCCCCH	37.20	21890473
65	Acetylation	NRQFLFQKKHVGRSK CHHHHHCCCCCCCCH	37.20	25953088
65	Ubiquitination	NRQFLFQKKHVGRSK CHHHHHCCCCCCCCH	37.20	21906983
66	Ubiquitination	RQFLFQKKHVGRSKA HHHHHCCCCCCCCHH	32.51	22817900
68	Ubiquitination	FLFQKKHVGRSKAQV HHHCCCCCCCCHHHH	10.53	-
72	Ubiquitination	KKHVGRSKAQVAKES CCCCCCCHHHHHHHH	41.29	22817900
77	Ubiquitination	RSKAQVAKESVLQFY CCHHHHHHHHHHHHC	52.22	21890473
77	2-Hydroxyisobutyrylation	RSKAQVAKESVLQFY CCHHHHHHHHHHHHC	52.22	-
77	Acetylation	RSKAQVAKESVLQFY CCHHHHHHHHHHHHC	52.22	23954790
77	Ubiquitination	RSKAQVAKESVLQFY CCHHHHHHHHHHHHC	52.22	21906983
84	Phosphorylation	KESVLQFYPKANIVA HHHHHHHCCCCCEEE	7.29	29759185
86	Ubiquitination	SVLQFYPKANIVAYH HHHHHCCCCCEEEEE	42.56	-
97	Sulfoxidation	VAYHDSIMNPDYNVE EEEECCCCCCCCCHH	7.44	30846556
145	Ubiquitination	ESGTAGYLGQVTTIK ECCCCCCCCCEEEEC	3.65	-
149	Ubiquitination	AGYLGQVTTIKKGVT CCCCCCEEEECCCCC	18.21	-
152	Sumoylation	LGQVTTIKKGVTECY CCCEEEECCCCCCCE	41.19	-
152	Ubiquitination	LGQVTTIKKGVTECY CCCEEEECCCCCCCE	41.19	32015554
153	Ubiquitination	GQVTTIKKGVTECYE CCEEEECCCCCCCEE	55.55	33845483
156	Phosphorylation	TTIKKGVTECYECHP EEECCCCCCCEECCC	29.07	28152594
157	Ubiquitination	TIKKGVTECYECHPK EECCCCCCCEECCCC	32.47	-
159	Phosphorylation	KKGVTECYECHPKPT CCCCCCCEECCCCCC	18.50	28152594
161	Ubiquitination	GVTECYECHPKPTQR CCCCCEECCCCCCCC	2.41	-
164	Ubiquitination	ECYECHPKPTQRTFP CCEECCCCCCCCCCC	36.71	-
164	Acetylation	ECYECHPKPTQRTFP CCEECCCCCCCCCCC	36.71	26822725
164	Sumoylation	ECYECHPKPTQRTFP CCEECCCCCCCCCCC	36.71	25114211
164	Ubiquitination	ECYECHPKPTQRTFP CCEECCCCCCCCCCC	36.71	33845483
166	Phosphorylation	YECHPKPTQRTFPGC EECCCCCCCCCCCCC	36.49	28152594
175	Acetylation	RTFPGCTIRNTPSEP CCCCCCEECCCCCCC	3.58	-
175	Methylation	RTFPGCTIRNTPSEP CCCCCCEECCCCCCC	3.58	-
175	Ubiquitination	RTFPGCTIRNTPSEP CCCCCCEECCCCCCC	3.58	-
177	Ubiquitination	FPGCTIRNTPSEPIH CCCCEECCCCCCCCH	53.11	21890473
178	Phosphorylation	PGCTIRNTPSEPIHC CCCEECCCCCCCCHH	20.53	20873877
178	Ubiquitination	PGCTIRNTPSEPIHC CCCEECCCCCCCCHH	20.53	22817900
184	Ubiquitination	NTPSEPIHCIVWAKY CCCCCCCHHHHHHHH	13.13	22817900
189	Ubiquitination	PIHCIVWAKYLFNQL CCHHHHHHHHHHHHH	4.63	21890473
190	Sumoylation	IHCIVWAKYLFNQLF CHHHHHHHHHHHHHH	27.12	-
190	Sumoylation	IHCIVWAKYLFNQLF CHHHHHHHHHHHHHH	27.12	28112733
191	Phosphorylation	HCIVWAKYLFNQLFG HHHHHHHHHHHHHHC	14.58	26074081
207	Phosphorylation	EDADQEVSPDRADPE CCCCCCCCCCCCCHH	21.96	29255136
208	Ubiquitination	DADQEVSPDRADPEA CCCCCCCCCCCCHHH	40.04	22817900
210	Methylation	DQEVSPDRADPEAAW CCCCCCCCCCHHHHC	44.25	115493113
213	Ubiquitination	VSPDRADPEAAWEPT CCCCCCCHHHHCCCC	31.94	21890473
217	Ubiquitination	RADPEAAWEPTEAEA CCCHHHHCCCCHHHH	21.10	21890473
220	Ubiquitination	PEAAWEPTEAEARAR HHHHCCCCHHHHHHH	35.99	-
220	Phosphorylation	PEAAWEPTEAEARAR HHHHCCCCHHHHHHH	35.99	26074081
225	Ubiquitination	EPTEAEARARASNED CCCHHHHHHHHCCCC	18.99	21890473
228	Ubiquitination	EAEARARASNEDGDI HHHHHHHHCCCCCCC	18.74	-
229	Phosphorylation	AEARARASNEDGDIK HHHHHHHCCCCCCCE	34.89	22496350
229	Ubiquitination	AEARARASNEDGDIK HHHHHHHCCCCCCCE	34.89	21890473
232	Ubiquitination	RARASNEDGDIKRIS HHHHCCCCCCCEECC	65.40	23000965
236	Sumoylation	SNEDGDIKRISTKEW CCCCCCCEECCHHHH	48.71	-
236	Acetylation	SNEDGDIKRISTKEW CCCCCCCEECCHHHH	48.71	20167786
236	Sumoylation	SNEDGDIKRISTKEW CCCCCCCEECCHHHH	48.71	-
236	Ubiquitination	SNEDGDIKRISTKEW CCCCCCCEECCHHHH	48.71	32015554
240	Ubiquitination	GDIKRISTKEWAKST CCCEECCHHHHHHHH	30.52	-
241	Ubiquitination	DIKRISTKEWAKSTG CCEECCHHHHHHHHC	44.46	21890473
241	Acetylation	DIKRISTKEWAKSTG CCEECCHHHHHHHHC	44.46	20167786
241	Ubiquitination	DIKRISTKEWAKSTG CCEECCHHHHHHHHC	44.46	22817900
243	Ubiquitination	KRISTKEWAKSTGYD EECCHHHHHHHHCCC	15.56	21890473
245	Ubiquitination	ISTKEWAKSTGYDPV CCHHHHHHHHCCCHH	50.01	21890473
245	Ubiquitination	ISTKEWAKSTGYDPV CCHHHHHHHHCCCHH	50.01	21906983
247	Ubiquitination	TKEWAKSTGYDPVKL HHHHHHHHCCCHHHH	38.77	23000965
249	Phosphorylation	EWAKSTGYDPVKLFT HHHHHHCCCHHHHHH	19.70	-
249	Ubiquitination	EWAKSTGYDPVKLFT HHHHHHCCCHHHHHH	19.70	23000965
253	Ubiquitination	STGYDPVKLFTKLFK HHCCCHHHHHHHHHH	43.18	21890473
253	2-Hydroxyisobutyrylation	STGYDPVKLFTKLFK HHCCCHHHHHHHHHH	43.18	-
253	Acetylation	STGYDPVKLFTKLFK HHCCCHHHHHHHHHH	43.18	25953088
253	Neddylation	STGYDPVKLFTKLFK HHCCCHHHHHHHHHH	43.18	32015554
253	Sumoylation	STGYDPVKLFTKLFK HHCCCHHHHHHHHHH	43.18	-
253	Ubiquitination	STGYDPVKLFTKLFK HHCCCHHHHHHHHHH	43.18	23000965
257	Ubiquitination	DPVKLFTKLFKDDIR CHHHHHHHHHHHHHH	44.59	21890473
257	Sumoylation	DPVKLFTKLFKDDIR CHHHHHHHHHHHHHH	44.59	-
257	2-Hydroxyisobutyrylation	DPVKLFTKLFKDDIR CHHHHHHHHHHHHHH	44.59	-
257	Acetylation	DPVKLFTKLFKDDIR CHHHHHHHHHHHHHH	44.59	25953088
257	Sumoylation	DPVKLFTKLFKDDIR CHHHHHHHHHHHHHH	44.59	28112733
257	Ubiquitination	DPVKLFTKLFKDDIR CHHHHHHHHHHHHHH	44.59	23000965
260	2-Hydroxyisobutyrylation	KLFTKLFKDDIRYLL HHHHHHHHHHHHHHH	66.00	-
260	Acetylation	KLFTKLFKDDIRYLL HHHHHHHHHHHHHHH	66.00	25953088
260	Ubiquitination	KLFTKLFKDDIRYLL HHHHHHHHHHHHHHH	66.00	23000965
265	Phosphorylation	LFKDDIRYLLTMDKL HHHHHHHHHHHHHHH	13.34	22817900
271	Ubiquitination	RYLLTMDKLWRKRKP HHHHHHHHHHHHCCC	38.84	21890473
271	Sumoylation	RYLLTMDKLWRKRKP HHHHHHHHHHHHCCC	38.84	-
271	Acetylation	RYLLTMDKLWRKRKP HHHHHHHHHHHHCCC	38.84	19608861
271	Methylation	RYLLTMDKLWRKRKP HHHHHHHHHHHHCCC	38.84	23644510
271	Sumoylation	RYLLTMDKLWRKRKP HHHHHHHHHHHHCCC	38.84	28112733
271	Ubiquitination	RYLLTMDKLWRKRKP HHHHHHHHHHHHCCC	38.84	23000965
275	Sumoylation	TMDKLWRKRKPPVPL HHHHHHHHCCCCCCC	53.87	-
275	Sumoylation	TMDKLWRKRKPPVPL HHHHHHHHCCCCCCC	53.87	-
275	Ubiquitination	TMDKLWRKRKPPVPL HHHHHHHHCCCCCCC	53.87	23000965
277	Sumoylation	DKLWRKRKPPVPLDW HHHHHHCCCCCCCCH	57.62	-
277	Ubiquitination	DKLWRKRKPPVPLDW HHHHHHCCCCCCCCH	57.62	23000965
288	Ubiquitination	PLDWAEVQSQGEETN CCCHHHHHCCCCCCC	22.88	21890473
289	Phosphorylation	LDWAEVQSQGEETNA CCHHHHHCCCCCCCH	45.38	25159151
294	Phosphorylation	VQSQGEETNASDQQN HHCCCCCCCHHHHCC	31.61	25850435
296	Ubiquitination	SQGEETNASDQQNEP CCCCCCCHHHHCCCC	23.15	21890473
297	Phosphorylation	QGEETNASDQQNEPQ CCCCCCHHHHCCCCC	37.71	25850435
308	Sumoylation	NEPQLGLKDQQVLDV CCCCCCCCCHHHEEH	52.25	-
308	Ubiquitination	NEPQLGLKDQQVLDV CCCCCCCCCHHHEEH	52.25	21890473
313	Ubiquitination	GLKDQQVLDVKSYAR CCCCHHHEEHHHHHH	5.64	-
316	Ubiquitination	DQQVLDVKSYARLFS CHHHEEHHHHHHHHH	37.10	21890473
316	Sumoylation	DQQVLDVKSYARLFS CHHHEEHHHHHHHHH	37.10	-
316	2-Hydroxyisobutyrylation	DQQVLDVKSYARLFS CHHHEEHHHHHHHHH	37.10	-
316	Sumoylation	DQQVLDVKSYARLFS CHHHEEHHHHHHHHH	37.10	-
316	Ubiquitination	DQQVLDVKSYARLFS CHHHEEHHHHHHHHH	37.10	22817900
323	Phosphorylation	KSYARLFSKSIETLR HHHHHHHHHCHHHHH	30.04	24719451
324	Ubiquitination	SYARLFSKSIETLRV HHHHHHHHCHHHHHH	48.39	21890473
324	2-Hydroxyisobutyrylation	SYARLFSKSIETLRV HHHHHHHHCHHHHHH	48.39	-
324	Acetylation	SYARLFSKSIETLRV HHHHHHHHCHHHHHH	48.39	19608861
324	Malonylation	SYARLFSKSIETLRV HHHHHHHHCHHHHHH	48.39	32601280
324	Ubiquitination	SYARLFSKSIETLRV HHHHHHHHCHHHHHH	48.39	23000965
328	Phosphorylation	LFSKSIETLRVHLAE HHHHCHHHHHHHHHH	20.42	-
336	Ubiquitination	LRVHLAEKGDGAELI HHHHHHHCCCCCEEE	57.61	21890473
336	Acetylation	LRVHLAEKGDGAELI HHHHHHHCCCCCEEE	57.61	7493407
336	Ubiquitination	LRVHLAEKGDGAELI HHHHHHHCCCCCEEE	57.61	22817900
346	Ubiquitination	GAELIWDKDDPSAMD CCEEEECCCCHHHHH	49.38	29967540
348	Ubiquitination	ELIWDKDDPSAMDFV EEEECCCCHHHHHHH	44.81	22817900
352	Sulfoxidation	DKDDPSAMDFVTSAA CCCCHHHHHHHHHHH	4.88	30846556
353	Ubiquitination	KDDPSAMDFVTSAAN CCCHHHHHHHHHHHH	34.28	21890473
357	Ubiquitination	SAMDFVTSAANLRMH HHHHHHHHHHHHHHH	21.78	21890473
365	Ubiquitination	AANLRMHIFSMNMKS HHHHHHHHHHCCCCC	1.68	21890473
369	Ubiquitination	RMHIFSMNMKSRFDI HHHHHHCCCCCCCCH	33.27	21890473
371	Ubiquitination	HIFSMNMKSRFDIKS HHHHCCCCCCCCHHH	33.21	-
371	Sumoylation	HIFSMNMKSRFDIKS HHHHCCCCCCCCHHH	33.21	-
371	Sumoylation	HIFSMNMKSRFDIKS HHHHCCCCCCCCHHH	33.21	-
372	Ubiquitination	IFSMNMKSRFDIKSM HHHCCCCCCCCHHHH	27.66	23000965
376	Ubiquitination	NMKSRFDIKSMAGNI CCCCCCCHHHHCCCH	3.06	-
378	Phosphorylation	KSRFDIKSMAGNIIP CCCCCHHHHCCCHHH	17.75	22210691
383	Ubiquitination	IKSMAGNIIPAIATT HHHHCCCHHHHHHHH	3.79	21890473
387	Ubiquitination	AGNIIPAIATTNAVI CCCHHHHHHHHHHHH	2.69	23000965
389	Phosphorylation	NIIPAIATTNAVIAG CHHHHHHHHHHHHHH	17.92	22210691
389	Ubiquitination	NIIPAIATTNAVIAG CHHHHHHHHHHHHHH	17.92	23000965
390	Phosphorylation	IIPAIATTNAVIAGL HHHHHHHHHHHHHHH	16.50	22210691
392	Ubiquitination	PAIATTNAVIAGLIV HHHHHHHHHHHHHHH	7.63	21890473
409	Ubiquitination	GLKILSGKIDQCRTI CHHHHCCCCCEEEEE	39.47	-
409	2-Hydroxyisobutyrylation	GLKILSGKIDQCRTI CHHHHCCCCCEEEEE	39.47	-
409	Acetylation	GLKILSGKIDQCRTI CHHHHCCCCCEEEEE	39.47	25953088
409	Ubiquitination	GLKILSGKIDQCRTI CHHHHCCCCCEEEEE	39.47	32015554
415	Phosphorylation	GKIDQCRTIFLNKQP CCCCEEEEEECCCCC	24.57	22210691
420	Ubiquitination	CRTIFLNKQPNPRKK EEEEECCCCCCCCCC	70.09	21890473
420	Acetylation	CRTIFLNKQPNPRKK EEEEECCCCCCCCCC	70.09	26051181
420	Sumoylation	CRTIFLNKQPNPRKK EEEEECCCCCCCCCC	70.09	25114211
420	Ubiquitination	CRTIFLNKQPNPRKK EEEEECCCCCCCCCC	70.09	21906983
427	Ubiquitination	KQPNPRKKLLVPCAL CCCCCCCCEEEEECC	48.62	29967540
428	Ubiquitination	QPNPRKKLLVPCALD CCCCCCCEEEEECCC	6.99	21890473
436	Ubiquitination	LVPCALDPPNPNCYV EEEECCCCCCCCCEE	31.27	21890473
439	Ubiquitination	CALDPPNPNCYVCAS ECCCCCCCCCEEECC	37.73	21890473
442	Ubiquitination	DPPNPNCYVCASKPE CCCCCCCEEECCCCE	12.76	23000965
444	Ubiquitination	PNPNCYVCASKPEVT CCCCCEEECCCCEEE	1.11	21890473
447	Acetylation	NCYVCASKPEVTVRL CCEEECCCCEEEEEE	27.03	26051181
448	Ubiquitination	CYVCASKPEVTVRLN CEEECCCCEEEEEEE	38.50	21890473
467	Ubiquitination	TVLTLQDKIVKEKFA EEEEECHHHHHHHHE	36.12	21890473
467	2-Hydroxyisobutyrylation	TVLTLQDKIVKEKFA EEEEECHHHHHHHHE	36.12	-
467	Acetylation	TVLTLQDKIVKEKFA EEEEECHHHHHHHHE	36.12	25953088
467	Ubiquitination	TVLTLQDKIVKEKFA EEEEECHHHHHHHHE	36.12	23000965
470	Ubiquitination	TLQDKIVKEKFAMVA EECHHHHHHHHEEEC	59.67	23000965
472	Ubiquitination	QDKIVKEKFAMVAPD CHHHHHHHHEEECCC	32.48	21890473
472	Ubiquitination	QDKIVKEKFAMVAPD CHHHHHHHHEEECCC	32.48	23000965
486	Ubiquitination	DVQIEDGKGTILISS CEEEECCCEEEEEEC	66.26	32015554
492	Phosphorylation	GKGTILISSEEGETE CCEEEEEECCCCCCC	28.40	-
493	Phosphorylation	KGTILISSEEGETEA CEEEEEECCCCCCCC	32.45	-
504	2-Hydroxyisobutyrylation	ETEANNHKKLSEFGI CCCCCCCHHHHHHCC	58.49	-
504	Ubiquitination	ETEANNHKKLSEFGI CCCCCCCHHHHHHCC	58.49	32015554
505	Ubiquitination	TEANNHKKLSEFGIR CCCCCCHHHHHHCCC	50.09	29967540
507	Phosphorylation	ANNHKKLSEFGIRNG CCCCHHHHHHCCCCC	39.50	25159151
521	Acetylation	GSRLQADDFLQDYTL CCCCCHHHHHHHHHH	49.52	-
527	Acetylation	DDFLQDYTLLINILH HHHHHHHHHHHHHHC	24.31	-
532	Ubiquitination	DYTLLINILHSEDLG HHHHHHHHHCHHHCC	2.65	21890473
540	Sumoylation	LHSEDLGKDVEFEVV HCHHHCCCCCEEEEE	66.93	-
540	Sumoylation	LHSEDLGKDVEFEVV HCHHHCCCCCEEEEE	66.93	28112733
553	Sumoylation	VVGDAPEKVGPKQAE EECCCCCCCCHHHHH	51.97	-
553	Ubiquitination	VVGDAPEKVGPKQAE EECCCCCCCCHHHHH	51.97	33845483
557	Ubiquitination	APEKVGPKQAEDAAK CCCCCCHHHHHHHHH	57.10	29967540
565	Phosphorylation	QAEDAAKSITNGSDD HHHHHHHHHHCCCCC	29.89	21406692
567	Phosphorylation	EDAAKSITNGSDDGA HHHHHHHHCCCCCCC	40.39	21406692
570	Phosphorylation	AKSITNGSDDGAQPS HHHHHCCCCCCCCCC	34.30	21406692
577	Phosphorylation	SDDGAQPSTSTAQEQ CCCCCCCCCCCCCCC	23.94	21406692
578	Phosphorylation	DDGAQPSTSTAQEQD CCCCCCCCCCCCCCC	36.46	30278072
579	Phosphorylation	DGAQPSTSTAQEQDD CCCCCCCCCCCCCCC	26.53	30278072
579	Ubiquitination	DGAQPSTSTAQEQDD CCCCCCCCCCCCCCC	26.53	21890473
580	Phosphorylation	GAQPSTSTAQEQDDV CCCCCCCCCCCCCCE	32.23	21406692
582	Ubiquitination	QPSTSTAQEQDDVLI CCCCCCCCCCCCEEE	49.31	23000965
584	Ubiquitination	STSTAQEQDDVLIVD CCCCCCCCCCEEEEC	39.87	21890473
592	Phosphorylation	DDVLIVDSDEEDSSN CCEEEECCCCCCCCC	35.71	26503892
595	Ubiquitination	LIVDSDEEDSSNNAD EEECCCCCCCCCCCC	69.09	24816145
597	Phosphorylation	VDSDEEDSSNNADVS ECCCCCCCCCCCCCC	37.94	30278072
598	Phosphorylation	DSDEEDSSNNADVSE CCCCCCCCCCCCCCH	46.56	30278072
604	Phosphorylation	SSNNADVSEEERSRK CCCCCCCCHHHHHHH	39.58	26074081
609	Phosphorylation	DVSEEERSRKRKLDE CCCHHHHHHHHHCCH	45.49	26074081
611	Sumoylation	SEEERSRKRKLDEKE CHHHHHHHHHCCHHH	55.95	-
611	Sumoylation	SEEERSRKRKLDEKE CHHHHHHHHHCCHHH	55.95	-
613	Sumoylation	EERSRKRKLDEKENL HHHHHHHHCCHHHHH	64.42	-
613	Acetylation	EERSRKRKLDEKENL HHHHHHHHCCHHHHH	64.42	-
613	Sumoylation	EERSRKRKLDEKENL HHHHHHHHCCHHHHH	64.42	-
617	Sumoylation	RKRKLDEKENLSAKR HHHHCCHHHHHHHHH	52.12	-
617	Acetylation	RKRKLDEKENLSAKR HHHHCCHHHHHHHHH	52.12	23749302
617	Sumoylation	RKRKLDEKENLSAKR HHHHCCHHHHHHHHH	52.12	19608861
617	Ubiquitination	RKRKLDEKENLSAKR HHHHCCHHHHHHHHH	52.12	19608861
621	Phosphorylation	LDEKENLSAKRSRIE CCHHHHHHHHHHHHH	43.24	24719451
623	Sumoylation	EKENLSAKRSRIEQK HHHHHHHHHHHHHHH	47.75	-
623	2-Hydroxyisobutyrylation	EKENLSAKRSRIEQK HHHHHHHHHHHHHHH	47.75	-
623	Acetylation	EKENLSAKRSRIEQK HHHHHHHHHHHHHHH	47.75	23749302
623	Sumoylation	EKENLSAKRSRIEQK HHHHHHHHHHHHHHH	47.75	-
623	Ubiquitination	EKENLSAKRSRIEQK HHHHHHHHHHHHHHH	47.75	24816145
625	Phosphorylation	ENLSAKRSRIEQKEE HHHHHHHHHHHHHHH	36.58	27251275
630	Sumoylation	KRSRIEQKEELDDVI HHHHHHHHHHHCCCC	40.12	-
630	Sumoylation	KRSRIEQKEELDDVI HHHHHHHHHHHCCCC	40.12	-
683	Ubiquitination	-------------------------------------------------- --------------------------------------------------		24816145
735	Ubiquitination	------------------------------------------------------------------------------------------------------ ------------------------------------------------------------------------------------------------------		24816145

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 SAE2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
236	K	Sumoylation		22403398
Sumoylation at Lys-236 inhibits enzymatic activity.

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 SAE2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SAE1_HUMAN	SAE1	physical	16189514
UBC9_HUMAN	UBE2I	physical	18691969
ETV4_HUMAN	ETV4	physical	19307308
SUMO1_HUMAN	SUMO1	physical	14673145
UBQL2_HUMAN	UBQLN2	physical	22939629
THADA_HUMAN	THADA	physical	22939629
SAHH2_HUMAN	AHCYL1	physical	22939629
SRSF2_HUMAN	SRSF2	physical	22939629
SPS2_HUMAN	SEPHS2	physical	22939629
TRIP6_HUMAN	TRIP6	physical	22939629
UNK_HUMAN	UNK	physical	22939629
ANCHR_HUMAN	ZFYVE19	physical	22939629
UBP34_HUMAN	USP34	physical	22939629
YAP1_HUMAN	YAP1	physical	22939629
ST1A1_HUMAN	SULT1A1	physical	22939629
UBE2B_HUMAN	UBE2B	physical	22939629
SHOT1_HUMAN	KIAA1598	physical	22939629
STMN2_HUMAN	STMN2	physical	22939629
TACC3_HUMAN	TACC3	physical	22939629
SYUG_HUMAN	SNCG	physical	22939629
TLE3_HUMAN	TLE3	physical	22939629
TTC9C_HUMAN	TTC9C	physical	22939629
TM1L2_HUMAN	TOM1L2	physical	22939629
SRXN1_HUMAN	SRXN1	physical	22939629
VATB2_HUMAN	ATP6V1B2	physical	22939629
UBC9_HUMAN	UBE2I	physical	12641448
CALU_HUMAN	CALU	physical	22863883
CATC_HUMAN	CTSC	physical	22863883
PDIA1_HUMAN	P4HB	physical	22863883
PDE12_HUMAN	PDE12	physical	22863883
PDLI5_HUMAN	PDLIM5	physical	22863883
RD23B_HUMAN	RAD23B	physical	22863883
SAE1_HUMAN	SAE1	physical	22863883
LA_HUMAN	SSB	physical	22863883
TCAL4_HUMAN	TCEAL4	physical	22863883
UBC9_HUMAN	UBE2I	physical	19250909
SUMO1_HUMAN	SUMO1	physical	9920803
UBC9_HUMAN	UBE2I	physical	9920803
FOXK1_HUMAN	FOXK1	physical	26344197
PSA3_HUMAN	PSMA3	physical	26344197
PSA4_HUMAN	PSMA4	physical	26344197
PSB3_HUMAN	PSMB3	physical	26344197
SAE1_HUMAN	SAE1	physical	26344197
WDR11_HUMAN	WDR11	physical	26344197
CHK1_HUMAN	CHEK1	physical	26296656
SAE1_HUMAN	SAE1	physical	28514442

Drug and Disease Associations

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

Regulatory Network of SAE2_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-271; LYS-324 AND LYS-617,AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-592, AND MASSSPECTROMETRY.	19413330 [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-592, AND MASSSPECTROMETRY.	18669648 [Abstract]

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