dbPTM

PSA2_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PSA2_RAT
UniProt AC	P17220
Protein Name	Proteasome subunit alpha type-2
Gene Name	Psma2
Organism	Rattus norvegicus (Rat).
Sequence Length	234
Subcellular Localization	Cytoplasm . Nucleus . Colocalizes with TRIM5 in cytoplasmic bodies.
Protein Description	Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex)..
Protein Sequence	MAERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAANGVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPDYRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYTQSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATAMGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQMTEDNIEVGICNEAGFRRLTPTEVRDYLAAIA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAERGYSFS ------CCCCCCEEE	18.39	2335242
6	Phosphorylation	--MAERGYSFSLTTF --CCCCCCEEEEEEE	16.86	-
7	Phosphorylation	-MAERGYSFSLTTFS -CCCCCCEEEEEEEC	15.93	27097102
9	Phosphorylation	AERGYSFSLTTFSPS CCCCCEEEEEEECCC	20.90	28432305
11	Phosphorylation	RGYSFSLTTFSPSGK CCCEEEEEEECCCCC	25.29	28432305
12	Phosphorylation	GYSFSLTTFSPSGKL CCEEEEEEECCCCCE	27.66	28432305
14	Phosphorylation	SFSLTTFSPSGKLVQ EEEEEEECCCCCEEE	18.96	28432305
16	Phosphorylation	SLTTFSPSGKLVQIE EEEEECCCCCEEEEH	47.57	28432305
24	Phosphorylation	GKLVQIEYALAAVAG CCEEEEHHHHHHHHC	14.45	-
51	Acetylation	VVLATEKKQKSILYD EEEEECCCCCCCCCC	57.64	22902405
53	Acetylation	LATEKKQKSILYDER EEECCCCCCCCCCCC	48.63	22902405
57	Phosphorylation	KKQKSILYDERSVHK CCCCCCCCCCCCCCC	17.68	30181290
64	Acetylation	YDERSVHKVEPITKH CCCCCCCCCCCCHHH	46.25	22902405
70	Acetylation	HKVEPITKHIGLVYS CCCCCCHHHEEEEEC	33.66	-
70	Ubiquitination	HKVEPITKHIGLVYS CCCCCCHHHEEEEEC	33.66	-
76	Phosphorylation	TKHIGLVYSGMGPDY HHHEEEEECCCCCCH	12.44	-
92	Acetylation	VLVHRARKLAQQYYL HHHHHHHHHHHHHHE	47.38	22902405
98	Phosphorylation	RKLAQQYYLVYQEPI HHHHHHHHEEECCCC	5.83	-
101	Phosphorylation	AQQYYLVYQEPIPTA HHHHHEEECCCCCHH	12.45	-
121	Phosphorylation	VASVMQEYTQSGGVR HHHHHHHHHHCCCCC	8.00	8794741
167	Phosphorylation	ATAMGKNYVNGKTFL EEECCCCCCCCEEHH	9.97	-
171	Acetylation	GKNYVNGKTFLEKRY CCCCCCCEEHHHHHH	30.79	22902405

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 PSA2_RAT !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PSA2_RAT !!

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 PSA2_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KCC2A_RAT	Camk2a	physical	19638347
HOME3_RAT	Homer3	physical	22486777
PRS8_RAT	Psmc5	physical	22486777
GRM1_RAT	Grm1	physical	22486777

Drug and Disease Associations

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

Regulatory Network of PSA2_RAT

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"The NH2-terminal residues of rat liver proteasome (multicatalyticproteinase complex) subunits, C2, C3 and C8, are N alpha-acetylated."; Tokunaga F., Aruga R., Iwanaga S., Tanaka K., Ichihara A., Takao T.,Shimonishi Y.; FEBS Lett. 263:373-375(1990). Cited for: PROTEIN SEQUENCE OF 2-30.	2335242 [Abstract]