SUMO3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SUMO3_HUMAN
• UniProt AC: P55854
• Protein Name: Small ubiquitin-related modifier 3 {ECO:0000305}
• Gene Name: SUMO3 {ECO:0000312|HGNC:HGNC:11124}
• Organism: Homo sapiens (Human).
• Sequence Length: 103
• Subcellular Localization: Cytoplasm. Nucleus. Nucleus, PML body.
• Protein Description: Ubiquitin-like protein which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Covalent attachment to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4. [PubMed: 11451954]
• Protein Sequence: MSEEKPKEGVKTENDHINLKVAGQDGSVVQFKIKRHTPLSKLMKAYCERQGLSMRQIRFRFDGQPINETDTPAQLEMEDEDTIDVFQQQTGGVPESSLAGHSF

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
2	Phosphorylation	------MSEEKPKEG ------CCCCCCCCC	55.23	25849741
5	Sumoylation	---MSEEKPKEGVKT ---CCCCCCCCCCCC	58.29	28112733
5	Ubiquitination	---MSEEKPKEGVKT ---CCCCCCCCCCCC	58.29	22505724
7	Sumoylation	-MSEEKPKEGVKTEN -CCCCCCCCCCCCCC	77.49	-
7	Ubiquitination	-MSEEKPKEGVKTEN -CCCCCCCCCCCCCC	77.49	22505724
7	Sumoylation	-MSEEKPKEGVKTEN -CCCCCCCCCCCCCC	77.49	28112733
11	Sumoylation	EKPKEGVKTENDHIN CCCCCCCCCCCCCEE	62.06	28112733
11	Ubiquitination	EKPKEGVKTENDHIN CCCCCCCCCCCCCEE	62.06	21890473
11	Ubiquitination	EKPKEGVKTENDHIN CCCCCCCCCCCCCEE	62.06	21963094
11	Sumoylation	EKPKEGVKTENDHIN CCCCCCCCCCCCCEE	62.06	-
11	Acetylation	EKPKEGVKTENDHIN CCCCCCCCCCCCCEE	62.06	23954790
12	Phosphorylation	KPKEGVKTENDHINL CCCCCCCCCCCCEEE	37.30	23186163
20	Acetylation	ENDHINLKVAGQDGS CCCCEEEEEECCCCC	26.08	26051181
20	Ubiquitination	ENDHINLKVAGQDGS CCCCEEEEEECCCCC	26.08	23000965
20	Sumoylation	ENDHINLKVAGQDGS CCCCEEEEEECCCCC	26.08	-
27	Phosphorylation	KVAGQDGSVVQFKIK EEECCCCCEEEEEEE	27.66	30266825
32	Malonylation	DGSVVQFKIKRHTPL CCCEEEEEEEECCHH	30.17	26320211
32	Ubiquitination	DGSVVQFKIKRHTPL CCCEEEEEEEECCHH	30.17	21890473
32	Neddylation	DGSVVQFKIKRHTPL CCCEEEEEEEECCHH	30.17	32015554
32	Sumoylation	DGSVVQFKIKRHTPL CCCEEEEEEEECCHH	30.17	-
32	Ubiquitination	DGSVVQFKIKRHTPL CCCEEEEEEEECCHH	30.17	23000965
32	Sumoylation	DGSVVQFKIKRHTPL CCCEEEEEEEECCHH	30.17	-
32	Methylation	DGSVVQFKIKRHTPL CCCEEEEEEEECCHH	30.17	72586755
32	Acetylation	DGSVVQFKIKRHTPL CCCEEEEEEEECCHH	30.17	23749302
34	Acetylation	SVVQFKIKRHTPLSK CEEEEEEEECCHHHH	38.42	25953088
34	Ubiquitination	SVVQFKIKRHTPLSK CEEEEEEEECCHHHH	38.42	21890473
34	Ubiquitination	SVVQFKIKRHTPLSK CEEEEEEEECCHHHH	38.42	23000965
34	Sumoylation	SVVQFKIKRHTPLSK CEEEEEEEECCHHHH	38.42	-
34	Neddylation	SVVQFKIKRHTPLSK CEEEEEEEECCHHHH	38.42	32015554
37	Phosphorylation	QFKIKRHTPLSKLMK EEEEEECCHHHHHHH	29.92	28152594
40	Phosphorylation	IKRHTPLSKLMKAYC EEECCHHHHHHHHHH	25.58	28152594
41	Acetylation	KRHTPLSKLMKAYCE EECCHHHHHHHHHHH	61.35	23749302
41	Neddylation	KRHTPLSKLMKAYCE EECCHHHHHHHHHHH	61.35	32015554
41	Ubiquitination	KRHTPLSKLMKAYCE EECCHHHHHHHHHHH	61.35	21890473
41	Sumoylation	KRHTPLSKLMKAYCE EECCHHHHHHHHHHH	61.35	-
41	Ubiquitination	KRHTPLSKLMKAYCE EECCHHHHHHHHHHH	61.35	23000965
41	Sumoylation	KRHTPLSKLMKAYCE EECCHHHHHHHHHHH	61.35	-
41	Malonylation	KRHTPLSKLMKAYCE EECCHHHHHHHHHHH	61.35	26320211
44	Malonylation	TPLSKLMKAYCERQG CHHHHHHHHHHHHCC	46.79	26320211
44	Ubiquitination	TPLSKLMKAYCERQG CHHHHHHHHHHHHCC	46.79	21890473
44	Sumoylation	TPLSKLMKAYCERQG CHHHHHHHHHHHHCC	46.79	-
44	Neddylation	TPLSKLMKAYCERQG CHHHHHHHHHHHHCC	46.79	32015554
44	Sumoylation	TPLSKLMKAYCERQG CHHHHHHHHHHHHCC	46.79	-
44	Methylation	TPLSKLMKAYCERQG CHHHHHHHHHHHHCC	46.79	14877669
44	Acetylation	TPLSKLMKAYCERQG CHHHHHHHHHHHHCC	46.79	19608861
44	Ubiquitination	TPLSKLMKAYCERQG CHHHHHHHHHHHHCC	46.79	23000965
49	Methylation	LMKAYCERQGLSMRQ HHHHHHHHCCCCCEE	32.10	-
53	Phosphorylation	YCERQGLSMRQIRFR HHHHCCCCCEEEEEE	20.81	30377224
82	Phosphorylation	LEMEDEDTIDVFQQQ ECCCCCCCEEHHHHH	19.61	24732914
90	Phosphorylation	IDVFQQQTGGVPESS EEHHHHHHCCCCHHH	31.40	24732914

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

Oops, there are no upstream regulatory protein records of SUMO3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SUMO3_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of SUMO3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
VIME_HUMAN	VIM	physical	16169070
SAE2_HUMAN	UBA2	physical	16620772
UBC9_HUMAN	UBE2I	physical	16620772
CAF1A_HUMAN	CHAF1A	physical	19919826
PML_HUMAN	PML	physical	21779164
UBP25_HUMAN	USP25	physical	18538659
UBC9_HUMAN	UBE2I	physical	21949651
USPL1_HUMAN	USPL1	physical	22878415
USPL1_DANRE	uspl1	physical	22878415
PIAS1_HUMAN	PIAS1	physical	16524884
PIAS2_HUMAN	PIAS2	physical	16524884
UBC9_HUMAN	UBE2I	physical	16524884
TYDP2_HUMAN	TDP2	physical	16524884
PIAS3_HUMAN	PIAS3	physical	16524884
SP100_HUMAN	SP100	physical	16524884
ORF50_HHV8P	ORF50	physical	23990779
IRF7_HUMAN	IRF7	physical	24267727
USPL1_HUMAN	USPL1	physical	25416956
SENP2_HUMAN	SENP2	physical	25416956
RN111_HUMAN	RNF111	physical	23530056
HIPK2_HUMAN	HIPK2	physical	21145359
ALDOB_HUMAN	ALDOB	physical	26344197
ECHM_HUMAN	ECHS1	physical	26344197
INO1_HUMAN	ISYNA1	physical	26344197
MARE1_HUMAN	MAPRE1	physical	26344197
PLPHP_HUMAN	PROSC	physical	26344197
SC23B_HUMAN	SEC23B	physical	26344197
TAGL2_HUMAN	TAGLN2	physical	26344197
TAGL3_HUMAN	TAGLN3	physical	26344197
UCHL3_HUMAN	UCHL3	physical	26344197
RNF8_HUMAN	RNF8	physical	28983621

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.

Related Literatures of Post-Translational Modification

Acetylation

"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-11; LYS-41 AND LYS-44, ANDMASS SPECTROMETRY.
PubMed: 19608861

Sumoylation

"Polymeric chains of SUMO-2 and SUMO-3 are conjugated to proteinsubstrates by SAE1/SAE2 and Ubc9.";
Tatham M.H., Jaffray E., Vaughan O.A., Desterro J.M.P., Botting C.H.,Naismith J.H., Hay R.T.;
J. Biol. Chem. 276:35368-35374(2001).
Cited for: FUNCTION IN SUMOYLATION OF PML, POLYSUMOYLATION, INTERACTION WITH SAE1AND UBE2I, SUMOYLATION AT LYS-11, MASS SPECTROMETRY, AND MUTAGENESISOF LYS-11.
PubMed: 11451954