dbPTM

PSB9_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PSB9_HUMAN
UniProt AC	P28065
Protein Name	Proteasome subunit beta type-9
Gene Name	PSMB9
Organism	Homo sapiens (Human).
Sequence Length	219
Subcellular Localization	Cytoplasm . Nucleus.
Protein Description	The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. Replacement of PSMB6 by PSMB9 increases the capacity of the immunoproteasome to cleave model peptides after hydrophobic and basic residues..
Protein Sequence	MLRAGAPTGDLPRAGEVHTGTTIMAVEFDGGVVMGSDSRVSAGEAVVNRVFDKLSPLHERIYCALSGSAADAQAVADMAAYQLELHGIELEEPPLVLAAANVVRNISYKYREDLSAHLMVAGWDQREGGQVYGTLGGMLTRQPFAIGGSGSTFIYGYVDAAYKPGMSPEECRRFTTDAIALAMSRDGSSGGVIYLVTITAAGVDHRVILGNELPKFYDE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Methylation	-----MLRAGAPTGD -----CCCCCCCCCC	29.67	115384957
8	Phosphorylation	MLRAGAPTGDLPRAG CCCCCCCCCCCCCCC	42.67	24719451
9 (in isoform 2)	Phosphorylation	-	33.14	24275569
21	Phosphorylation	AGEVHTGTTIMAVEF CCCCCCCCEEEEEEE	17.82	24275569
38	Phosphorylation	GVVMGSDSRVSAGEA CEEECCCCCCCCCHH	35.96	24275569
43 (in isoform 2)	Ubiquitination	-	18.85	21890473
53	Acetylation	VVNRVFDKLSPLHER HHHHHHHHCCHHHHH	39.12	19608861
53	Ubiquitination	VVNRVFDKLSPLHER HHHHHHHHCCHHHHH	39.12	21890473
53 (in isoform 1)	Ubiquitination	-	39.12	21890473
53	Ubiquitination	VVNRVFDKLSPLHER HHHHHHHHCCHHHHH	39.12	19608861
55	Phosphorylation	NRVFDKLSPLHERIY HHHHHHCCHHHHHHH	31.02	28450419
109	Ubiquitination	VVRNISYKYREDLSA HHHHCCHHHHCCHHH	30.92	19608861
109	Malonylation	VVRNISYKYREDLSA HHHHCCHHHHCCHHH	30.92	26320211
109	Acetylation	VVRNISYKYREDLSA HHHHCCHHHHCCHHH	30.92	19608861
140	Phosphorylation	GTLGGMLTRQPFAIG EEECCEEECCCEEEC	20.54	23879269
175	Phosphorylation	PEECRRFTTDAIALA HHHHHHCHHHHHHHH	23.19	24719451
188	Phosphorylation	LAMSRDGSSGGVIYL HHHCCCCCCCCEEEE	30.05	-
215	Ubiquitination	ILGNELPKFYDE--- EECCCCCCCCCC---	70.00	-
217	Phosphorylation	GNELPKFYDE----- CCCCCCCCCC-----	25.86	28796482

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 PSB9_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PSB9_HUMAN !!

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 PSB9_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SRC_HUMAN	SRC	physical	16957778
PRS8_HUMAN	PSMC5	physical	16957778
RPB1_HUMAN	POLR2A	physical	16957778
PSB5_HUMAN	PSMB5	physical	10816564
PSA7_HUMAN	PSMA7	physical	17506986
PSB8_HUMAN	PSMB8	physical	17506986
POMP_HUMAN	POMP	physical	17506986
PSB9_HUMAN	PSMB9	physical	11602734
NCOA2_HUMAN	NCOA2	physical	16957778
NCOA3_HUMAN	NCOA3	physical	16957778
ESR1_HUMAN	ESR1	physical	16957778
RPB2_HUMAN	POLR2B	physical	16957778
RPB3_HUMAN	POLR2C	physical	16957778
RPB4_HUMAN	POLR2D	physical	16957778
RPAB1_HUMAN	POLR2E	physical	16957778
RPAB2_HUMAN	POLR2F	physical	16957778
RPB7_HUMAN	POLR2G	physical	16957778
RPAB3_HUMAN	POLR2H	physical	16957778
RPB9_HUMAN	POLR2I	physical	16957778
RPAB5_HUMAN	POLR2L	physical	16957778
RPB11_HUMAN	POLR2J	physical	16957778
RPAB4_HUMAN	POLR2K	physical	16957778
ELOA1_HUMAN	TCEB3	physical	16957778
PSMD1_HUMAN	PSMD1	physical	26186194
PSD13_HUMAN	PSMD13	physical	26186194
PSA2_HUMAN	PSMA2	physical	26186194
UBP15_HUMAN	USP15	physical	26186194
PSA3_HUMAN	PSMA3	physical	26186194
PSB1_HUMAN	PSMB1	physical	26186194
PSA6_HUMAN	PSMA6	physical	26186194
PSMD3_HUMAN	PSMD3	physical	26186194
PSME4_HUMAN	PSME4	physical	26186194
PSA7L_HUMAN	PSMA8	physical	26186194
PSA7_HUMAN	PSMA7	physical	26186194
PSD11_HUMAN	PSMD11	physical	26186194
PRS10_HUMAN	PSMC6	physical	26186194
PRS6A_HUMAN	PSMC3	physical	26186194
PSB2_HUMAN	PSMB2	physical	26186194
PSME1_HUMAN	PSME1	physical	26186194
PRS6B_HUMAN	PSMC4	physical	26186194
PRS8_HUMAN	PSMC5	physical	26186194
PSMD2_HUMAN	PSMD2	physical	26186194
OSER1_HUMAN	OSER1	physical	26186194
PSDE_HUMAN	PSMD14	physical	26186194
POMP_HUMAN	POMP	physical	26186194
PRS7_HUMAN	PSMC2	physical	26186194
SEMG1_HUMAN	SEMG1	physical	26186194
PSMD8_HUMAN	PSMD8	physical	26186194
PSMD7_HUMAN	PSMD7	physical	26186194
PSD12_HUMAN	PSMD12	physical	26186194
PSMD6_HUMAN	PSMD6	physical	26186194
PSA5_HUMAN	PSMA5	physical	26186194
UCHL5_HUMAN	UCHL5	physical	26186194
PSA4_HUMAN	PSMA4	physical	26186194
PSME3_HUMAN	PSME3	physical	26186194
PSME2_HUMAN	PSME2	physical	26186194
KCRM_HUMAN	CKM	physical	26186194
PSB5_HUMAN	PSMB5	physical	26186194
PSB3_HUMAN	PSMB3	physical	26186194
PSMG1_HUMAN	PSMG1	physical	26186194
F192A_HUMAN	FAM192A	physical	26186194
PSMD4_HUMAN	PSMD4	physical	26186194
PSMG3_HUMAN	PSMG3	physical	26186194
RN181_HUMAN	RNF181	physical	26186194
PSMF1_HUMAN	PSMF1	physical	26186194
FBX7_HUMAN	FBXO7	physical	26186194
PSMG4_HUMAN	PSMG4	physical	26186194
PSB10_HUMAN	PSMB10	physical	26186194
PSB2_HUMAN	PSMB2	physical	26344197
PSA7L_HUMAN	PSMA8	physical	28514442
POMP_HUMAN	POMP	physical	28514442
PSME2_HUMAN	PSME2	physical	28514442
PSME4_HUMAN	PSME4	physical	28514442
PSME1_HUMAN	PSME1	physical	28514442
KCRM_HUMAN	CKM	physical	28514442
PSMG1_HUMAN	PSMG1	physical	28514442
PSMF1_HUMAN	PSMF1	physical	28514442
RN181_HUMAN	RNF181	physical	28514442
OSER1_HUMAN	OSER1	physical	28514442
PSMG3_HUMAN	PSMG3	physical	28514442
PSMG4_HUMAN	PSMG4	physical	28514442
PSA7_HUMAN	PSMA7	physical	28514442
PSA2_HUMAN	PSMA2	physical	28514442
PSD13_HUMAN	PSMD13	physical	28514442
PSA6_HUMAN	PSMA6	physical	28514442
PSD12_HUMAN	PSMD12	physical	28514442
PSD11_HUMAN	PSMD11	physical	28514442
PSA3_HUMAN	PSMA3	physical	28514442
PSMD6_HUMAN	PSMD6	physical	28514442
PSME3_HUMAN	PSME3	physical	28514442
PRS7_HUMAN	PSMC2	physical	28514442
PSDE_HUMAN	PSMD14	physical	28514442
PSB5_HUMAN	PSMB5	physical	28514442
PSMD1_HUMAN	PSMD1	physical	28514442
PSA5_HUMAN	PSMA5	physical	28514442
PSMD7_HUMAN	PSMD7	physical	28514442
PRS6A_HUMAN	PSMC3	physical	28514442
PSA4_HUMAN	PSMA4	physical	28514442
F192A_HUMAN	FAM192A	physical	28514442
PRS8_HUMAN	PSMC5	physical	28514442
PSMD4_HUMAN	PSMD4	physical	28514442
UBP15_HUMAN	USP15	physical	28514442
PSMD3_HUMAN	PSMD3	physical	28514442
PRS4_HUMAN	PSMC1	physical	28514442
PRS10_HUMAN	PSMC6	physical	28514442
PSB2_HUMAN	PSMB2	physical	28514442
PSMD2_HUMAN	PSMD2	physical	28514442
FBX7_HUMAN	FBXO7	physical	28514442
PRS6B_HUMAN	PSMC4	physical	28514442
PSMD8_HUMAN	PSMD8	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
DB08889	Carfilzomib

Regulatory Network of PSB9_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-53 AND LYS-109, AND MASSSPECTROMETRY.	19608861 [Abstract]