SAE2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SAE2_MOUSE
• UniProt AC: Q9Z1F9
• Protein Name: SUMO-activating enzyme subunit 2
• Gene Name: Uba2
• Organism: Mus musculus (Mouse).
• Sequence Length: 638
• 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 (By similarity)..
• Protein Sequence: MALSRGLPRELAEAVSGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFHPQANIEAHHDSIMNPDYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYECHPKPTQRTFPGCTIRNTPSEPIHCIVWAKYLFNQLFGEEDADQEVSPDRADPEAAWEPTEAEARARASNEDGDIKRISTKEWAKSTGYDPVKLFTKLFKDDIRYLLTMDKLWRKRKPPVPLDWAEVQSQGEANADQQNEPQLGLKDQQVLDVKSYASLFSKSIETLRVHLAEKGDGAELIWDKDDPPAMDFVTSAANLRMHIFSMNMKSRFDIKSMAGNIIPAIATTNAVIAGLIVLEGLKILSGKIDQCRTIFLNKQPNPRKKLLVPCALDPPNTNCYVCASKPEVTVRLNVHKVTVLTLQDKIVKEKFAMVAPDVQIEDGKGTILISSEEGETEANNPKKLSDFGIRNGSRLQADDFLQDYTLLINILHSEDLGKDVEFEVVGDSPEKVGPKQAEDAAKSIANGSDDGAQPSTSTAQEQDDVLIVDSDEEGPSNSTDCSGDDKARKRKLEENEAASTKKCRLEQMEDPDDVIALD

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Methylation	---MALSRGLPRELA ---CCCCCCCCHHHH	52.06	16189297
9	Methylation	ALSRGLPRELAEAVS CCCCCCCHHHHHHHC	57.51	16189305
16	Phosphorylation	RELAEAVSGGRVLVV HHHHHHHCCCEEEEE	42.45	-
65	Ubiquitination	NRQFLFQKKHVGRSK CHHHHHCCCCCCCCH	37.20	-
161	Glutathionylation	GVTECYECHPKPTQR CCCCCEECCCCCCCC	2.41	24333276
164	Sumoylation	ECYECHPKPTQRTFP CCEECCCCCCCCCCC	36.71	28289178
173	Glutathionylation	TQRTFPGCTIRNTPS CCCCCCCCEECCCCC	2.66	24333276
191	Phosphorylation	HCIVWAKYLFNQLFG HHHHHHHHHHHHHHC	14.58	23984901
207	Phosphorylation	EDADQEVSPDRADPE CCCCCCCCCCCCCHH	21.96	21082442
229	Phosphorylation	AEARARASNEDGDIK HHHHHHHCCCCCCCE	34.89	30635358
241	Ubiquitination	DIKRISTKEWAKSTG CCEECCHHHHHHHHC	44.46	27667366
245	Ubiquitination	ISTKEWAKSTGYDPV CCHHHHHHHHCCCHH	50.01	27667366
253	Ubiquitination	STGYDPVKLFTKLFK HHCCCHHHHHHHHHH	43.18	27667366
257	Ubiquitination	DPVKLFTKLFKDDIR CHHHHHHHHHHHHHH	44.59	27667366
257	Sumoylation	DPVKLFTKLFKDDIR CHHHHHHHHHHHHHH	44.59	28289178
260	Acetylation	KLFTKLFKDDIRYLL HHHHHHHHHHHHHHH	66.00	22826441
271	Acetylation	RYLLTMDKLWRKRKP HHHHHHHHHHHHCCC	38.84	23806337
289	Phosphorylation	LDWAEVQSQGEANAD CCHHHHHCCCCCCCC	45.38	25338131
322	Acetylation	SYASLFSKSIETLRV HHHHHHHHCHHHHHH	48.39	22826441
322	Ubiquitination	SYASLFSKSIETLRV HHHHHHHHCHHHHHH	48.39	-
334	Ubiquitination	LRVHLAEKGDGAELI HHHHHHHCCCCCEEE	57.61	-
354	Phosphorylation	PPAMDFVTSAANLRM CCHHHHHHHHHHHHH	16.79	28059163
355	Phosphorylation	PAMDFVTSAANLRMH CHHHHHHHHHHHHHH	21.78	28059163
365	Phosphorylation	NLRMHIFSMNMKSRF HHHHHHHHCCCCCCC	14.51	28059163
405	Phosphorylation	LEGLKILSGKIDQCR HHCHHHHCCCCCEEE	41.32	29895711
407	Acetylation	GLKILSGKIDQCRTI CHHHHCCCCCEEEEE	39.47	22826441
413	Phosphorylation	GKIDQCRTIFLNKQP CCCCEEEEEECCCCC	24.57	29899451
418	Acetylation	CRTIFLNKQPNPRKK EEEEECCCCCCCCCC	70.09	22826441
425	Acetylation	KQPNPRKKLLVPCAL CCCCCCCCEEEEECC	48.62	22826441
445	Acetylation	NCYVCASKPEVTVRL CEEEECCCCEEEEEE	27.03	22826441
465	Ubiquitination	TVLTLQDKIVKEKFA EEEEECHHHHHHHHE	36.12	-
486	Phosphorylation	QIEDGKGTILISSEE EEECCCEEEEEECCC	18.98	26525534
503	Ubiquitination	TEANNPKKLSDFGIR CCCCCCCCHHHHCCC	55.25	-
505	Phosphorylation	ANNPKKLSDFGIRNG CCCCCCHHHHCCCCC	39.51	24759943
548	Phosphorylation	EFEVVGDSPEKVGPK EEEEECCCHHHCCHH	29.09	25521595
563	Phosphorylation	QAEDAAKSIANGSDD HHHHHHHHHHCCCCC	23.39	26525534
568	Phosphorylation	AKSIANGSDDGAQPS HHHHHCCCCCCCCCC	32.13	26525534
575	Phosphorylation	SDDGAQPSTSTAQEQ CCCCCCCCCCCCCCC	23.94	23984901
576	Phosphorylation	DDGAQPSTSTAQEQD CCCCCCCCCCCCCCC	36.46	23984901
577	Phosphorylation	DGAQPSTSTAQEQDD CCCCCCCCCCCCCCC	26.53	23984901
578	Phosphorylation	GAQPSTSTAQEQDDV CCCCCCCCCCCCCCE	32.23	22668510
590	Phosphorylation	DDVLIVDSDEEGPSN CCEEEECCCCCCCCC	35.71	22942356
596	Phosphorylation	DSDEEGPSNSTDCSG CCCCCCCCCCCCCCC	55.03	25777480
598	Phosphorylation	DEEGPSNSTDCSGDD CCCCCCCCCCCCCCH	29.93	24453211
599	Phosphorylation	EEGPSNSTDCSGDDK CCCCCCCCCCCCCHH	45.32	25777480
602	Phosphorylation	PSNSTDCSGDDKARK CCCCCCCCCCHHHHH	48.33	21183079
611	Acetylation	DDKARKRKLEENEAA CHHHHHHHHHHHHHH	64.38	23806337
619	Phosphorylation	LEENEAASTKKCRLE HHHHHHHHCCCCCHH	48.05	-
621	Acetylation	ENEAASTKKCRLEQM HHHHHHCCCCCHHHC	47.59	130725

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of SAE2_MOUSE !!

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of SAE2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of SAE2_MOUSE !!

Drug and Disease Associations

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