UBAC1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: UBAC1_HUMAN
• UniProt AC: Q9BSL1
• Protein Name: Ubiquitin-associated domain-containing protein 1
• Gene Name: UBAC1
• Organism: Homo sapiens (Human).
• Sequence Length: 405
• Subcellular Localization: Cytoplasm .
• Protein Description: Non-catalytic subunit of the KPC complex that acts as E3 ubiquitin-protein ligase. Required for poly-ubiquitination and proteasome-mediated degradation of CDKN1B during G1 phase of the cell cycle..
• Protein Sequence: MFVQEEKIFAGKVLRLHICASDGAEWLEEATEDTSVEKLKERCLKHCAHGSLEDPKSITHHKLIHAASERVLSDARTILEENIQDQDVLLLIKKRAPSPLPKMADVSAEEKKKQDQKAPDKEAILRATANLPSYNMDRAAVQTNMRDFQTELRKILVSLIEVAQKLLALNPDAVELFKKANAMLDEDEDERVDEAALRQLTEMGFPENRATKALQLNHMSVPQAMEWLIEHAEDPTIDTPLPGQAPPEAEGATAAASEAAAGASATDEEARDELTEIFKKIRRKREFRADARAVISLMEMGFDEKEVIDALRVNNNQQNAACEWLLGDRKPSPEELDKGIDPDSPLFQAILDNPVVQLGLTNPKTLLAFEDMLENPLNSTQWMNDPETGPVMLQISRIFQTLNRT

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
1	Acetylation	-------MFVQEEKI -------CCCCCHHH	7.19	22814378
7	Ubiquitination	-MFVQEEKIFAGKVL -CCCCCHHHHCCCEE	42.23	21890473
12	Ubiquitination	EEKIFAGKVLRLHIC CHHHHCCCEEEEEEE	34.37	-
45	Ubiquitination	KLKERCLKHCAHGSL HHHHHHHHHCCCCCC	40.02	-
56	Ubiquitination	HGSLEDPKSITHHKL CCCCCCCCCCCHHHH	67.80	-
62	Ubiquitination	PKSITHHKLIHAASE CCCCCHHHHHHHHHH	41.34	-
68	Phosphorylation	HKLIHAASERVLSDA HHHHHHHHHHHHHHH	27.07	23312004
93	Ubiquitination	QDVLLLIKKRAPSPL CCEEEEEECCCCCCC	35.86	-
98	Phosphorylation	LIKKRAPSPLPKMAD EEECCCCCCCCCCCC	37.78	25159151
107	Phosphorylation	LPKMADVSAEEKKKQ CCCCCCCCHHHHHHH	30.43	26074081
111	Ubiquitination	ADVSAEEKKKQDQKA CCCCHHHHHHHHCCC	57.69	21890473
112	Ubiquitination	DVSAEEKKKQDQKAP CCCHHHHHHHHCCCC	59.97	-
117	Ubiquitination	EKKKQDQKAPDKEAI HHHHHHCCCCCHHHH	70.90	-
121	Ubiquitination	QDQKAPDKEAILRAT HHCCCCCHHHHHHHH	48.24	21890473
154	Ubiquitination	DFQTELRKILVSLIE HHHHHHHHHHHHHHH	53.68	21890473
178	Ubiquitination	PDAVELFKKANAMLD HHHHHHHHHHHHCCC	64.70	21890473
178	Acetylation	PDAVELFKKANAMLD HHHHHHHHHHHHCCC	64.70	24627041
179	Ubiquitination	DAVELFKKANAMLDE HHHHHHHHHHHCCCC	39.27	21890473
279	Ubiquitination	DELTEIFKKIRRKRE HHHHHHHHHHHHHHH	53.61	-
296	Phosphorylation	ADARAVISLMEMGFD HHHHHHHHHHHCCCC	18.31	22210691
305	Ubiquitination	MEMGFDEKEVIDALR HHCCCCHHHHHHHHH	60.16	-
330	Ubiquitination	EWLLGDRKPSPEELD HHHHCCCCCCHHHHH	55.37	21890473
332	Phosphorylation	LLGDRKPSPEELDKG HHCCCCCCHHHHHCC	48.23	26657352
338	Ubiquitination	PSPEELDKGIDPDSP CCHHHHHCCCCCCCH	71.09	-
344	Phosphorylation	DKGIDPDSPLFQAIL HCCCCCCCHHHHHHH	28.96	-

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
-	K	Ubiquitination	E3 ubiquitin ligase	SMURF1	Q9HCE7	PMID:20804422

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of UBAC1_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 UBAC1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CPSF6_HUMAN	CPSF6	physical	16189514
RN123_HUMAN	RNF123	physical	17353931
IQGA2_HUMAN	IQGAP2	physical	17353931
MYH2_HUMAN	MYH2	physical	17353931
RN123_HUMAN	RNF123	physical	16227581
PSMD4_HUMAN	PSMD4	physical	16227581
PSMD7_HUMAN	PSMD7	physical	16227581
PSMD6_HUMAN	PSMD6	physical	16227581
RN123_HUMAN	RNF123	physical	15746103
A4_HUMAN	APP	physical	21832049
UTP6_HUMAN	UTP6	physical	22939629
VPS25_HUMAN	VPS25	physical	22939629
UBP7_HUMAN	USP7	physical	22939629
TRIM2_HUMAN	TRIM2	physical	25416956
TRI39_HUMAN	TRIM39	physical	25416956
DVL2_HUMAN	DVL2	physical	21516116
TRIM2_HUMAN	TRIM2	physical	21516116
RS27A_HUMAN	RPS27A	physical	28514442
RN123_HUMAN	RNF123	physical	28514442
UBB_HUMAN	UBB	physical	28514442
BAP31_HUMAN	BCAP31	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.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-98, AND MASSSPECTROMETRY.
PubMed: 19413330