dbPTM

PRS6A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PRS6A_HUMAN
UniProt AC	P17980
Protein Name	26S proteasome regulatory subunit 6A
Gene Name	PSMC3
Organism	Homo sapiens (Human).
Sequence Length	439
Subcellular Localization	Cytoplasm . Nucleus . Colocalizes with TRIM5 in the cytoplasmic bodies.
Protein Description	Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC3 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides..
Protein Sequence	MNLLPNIESPVTRQEKMATVWDEAEQDGIGEEVLKMSTEEIIQRTRLLDSEIKIMKSEVLRVTHELQAMKDKIKENSEKIKVNKTLPYLVSNVIELLDVDPNDQEEDGANIDLDSQRKGKCAVIKTSTRQTYFLPVIGLVDAEKLKPGDLVGVNKDSYLILETLPTEYDSRVKAMEVDERPTEQYSDIGGLDKQIQELVEAIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDGAKLVRDAFALAKEKAPSIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFQPNTQVKVIAATNRVDILDPALLRSGRLDRKIEFPMPNEEARARIMQIHSRKMNVSPDVNYEELARCTDDFNGAQCKAVCVEAGMIALRRGATELTHEDYMEGILEVQAKKKANLQYYA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MNLLPNIE -------CCCCCCCC	7.81	20068231
9	Phosphorylation	NLLPNIESPVTRQEK CCCCCCCCCCCHHHH	22.37	29255136
12	Phosphorylation	PNIESPVTRQEKMAT CCCCCCCCHHHHHHH	29.98	29255136
16	Ubiquitination	SPVTRQEKMATVWDE CCCCHHHHHHHHHHH	26.04	21890473
19	Phosphorylation	TRQEKMATVWDEAEQ CHHHHHHHHHHHHHH	20.73	21601212
35	Ubiquitination	GIGEEVLKMSTEEII CCCHHHHHCCHHHHH	35.66	21890473
36	Sulfoxidation	IGEEVLKMSTEEIIQ CCHHHHHCCHHHHHH	5.39	30846556
37	Phosphorylation	GEEVLKMSTEEIIQR CHHHHHCCHHHHHHH	30.95	21815630
38	Phosphorylation	EEVLKMSTEEIIQRT HHHHHCCHHHHHHHH	33.85	29255136
45	Phosphorylation	TEEIIQRTRLLDSEI HHHHHHHHHHHHHHH	14.86	28787133
50	Phosphorylation	QRTRLLDSEIKIMKS HHHHHHHHHHHHCHH	40.99	21815630
53	Succinylation	RLLDSEIKIMKSEVL HHHHHHHHHCHHHHH	32.47	23954790
53	Ubiquitination	RLLDSEIKIMKSEVL HHHHHHHHHCHHHHH	32.47	21890473
53	2-Hydroxyisobutyrylation	RLLDSEIKIMKSEVL HHHHHHHHHCHHHHH	32.47	-
53	Acetylation	RLLDSEIKIMKSEVL HHHHHHHHHCHHHHH	32.47	25038526
56	Acetylation	DSEIKIMKSEVLRVT HHHHHHCHHHHHHHH	47.11	25953088
56	Ubiquitination	DSEIKIMKSEVLRVT HHHHHHCHHHHHHHH	47.11	21890473
61	Methylation	IMKSEVLRVTHELQA HCHHHHHHHHHHHHH	36.14	115492871
69	Sulfoxidation	VTHELQAMKDKIKEN HHHHHHHHHHHHHHC	3.58	30846556
70	Acetylation	THELQAMKDKIKENS HHHHHHHHHHHHHCH	59.91	25953088
70	Ubiquitination	THELQAMKDKIKENS HHHHHHHHHHHHHCH	59.91	21890473
70	2-Hydroxyisobutyrylation	THELQAMKDKIKENS HHHHHHHHHHHHHCH	59.91	-
72	Ubiquitination	ELQAMKDKIKENSEK HHHHHHHHHHHCHHH	50.59	-
74	Ubiquitination	QAMKDKIKENSEKIK HHHHHHHHHCHHHHC	57.49	-
79	Acetylation	KIKENSEKIKVNKTL HHHHCHHHHCCCCHH	47.88	25953088
79	Ubiquitination	KIKENSEKIKVNKTL HHHHCHHHHCCCCHH	47.88	-
84	Ubiquitination	SEKIKVNKTLPYLVS HHHHCCCCHHHHHHH	55.19	-
118	Ubiquitination	IDLDSQRKGKCAVIK CCCCCCCCCCEEEEE	55.90	-
125	Ubiquitination	KGKCAVIKTSTRQTY CCCEEEEECCCCCEE	29.80	-
125	Acetylation	KGKCAVIKTSTRQTY CCCEEEEECCCCCEE	29.80	25953088
131	Phosphorylation	IKTSTRQTYFLPVIG EECCCCCEEEEEEEE	16.98	-
132	Phosphorylation	KTSTRQTYFLPVIGL ECCCCCEEEEEEEEE	8.52	20090780
144	Ubiquitination	IGLVDAEKLKPGDLV EEEEEHHHCCCCCEE	64.63	21890473
146	Ubiquitination	LVDAEKLKPGDLVGV EEEHHHCCCCCEECC	59.01	21890473
155	Ubiquitination	GDLVGVNKDSYLILE CCEECCCCCCEEEEE	45.72	21890473
163	Phosphorylation	DSYLILETLPTEYDS CCEEEEECCCCCCHH	34.29	-
173	Ubiquitination	TEYDSRVKAMEVDER CCCHHHCEEEECCCC	40.69	21890473
175	Sulfoxidation	YDSRVKAMEVDERPT CHHHCEEEECCCCCC	4.23	30846556
182	Phosphorylation	MEVDERPTEQYSDIG EECCCCCCHHHCCCC	41.77	28796482
185	Phosphorylation	DERPTEQYSDIGGLD CCCCCHHHCCCCCHH	11.32	28796482
186	Phosphorylation	ERPTEQYSDIGGLDK CCCCHHHCCCCCHHH	23.57	28796482
193	Ubiquitination	SDIGGLDKQIQELVE CCCCCHHHHHHHHHH	55.11	-
206	Sulfoxidation	VEAIVLPMNHKEKFE HHHHHCCCCCHHHHH	7.79	30846556
209	Ubiquitination	IVLPMNHKEKFENLG HHCCCCCHHHHHHCC	58.56	21890473
211	Acetylation	LPMNHKEKFENLGIQ CCCCCHHHHHHCCCC	63.88	23954790
211	Ubiquitination	LPMNHKEKFENLGIQ CCCCCHHHHHHCCCC	63.88	21890473
221	Ubiquitination	NLGIQPPKGVLMYGP HCCCCCCCCEEEECC	69.23	-
225	Sulfoxidation	QPPKGVLMYGPPGTG CCCCCEEEECCCCCC	3.19	30846556
226	Phosphorylation	PPKGVLMYGPPGTGK CCCCEEEECCCCCCH	23.48	23917254
231	Phosphorylation	LMYGPPGTGKTLLAR EEECCCCCCHHHHHH	41.08	20068231
233	Ubiquitination	YGPPGTGKTLLARAC ECCCCCCHHHHHHHH	35.52	21890473
245	Ubiquitination	RACAAQTKATFLKLA HHHHHHCHHHHHHHH	33.09	21890473
245	Malonylation	RACAAQTKATFLKLA HHHHHHCHHHHHHHH	33.09	26320211
245	2-Hydroxyisobutyrylation	RACAAQTKATFLKLA HHHHHHCHHHHHHHH	33.09	-
245	Acetylation	RACAAQTKATFLKLA HHHHHHCHHHHHHHH	33.09	26051181
250	Ubiquitination	QTKATFLKLAGPQLV HCHHHHHHHHCHHHH	31.90	21890473
259	Sulfoxidation	AGPQLVQMFIGDGAK HCHHHHHHHHCCHHH	1.74	21406390
266	Ubiquitination	MFIGDGAKLVRDAFA HHHCCHHHHHHHHHH	53.71	21890473
276	Succinylation	RDAFALAKEKAPSII HHHHHHHHCCCCEEE	61.67	23954790
276	Ubiquitination	RDAFALAKEKAPSII HHHHHHHHCCCCEEE	61.67	-
278	Ubiquitination	AFALAKEKAPSIIFI HHHHHHCCCCEEEEE	65.96	21890473
278	2-Hydroxyisobutyrylation	AFALAKEKAPSIIFI HHHHHHCCCCEEEEE	65.96	-
294	2-Hydroxyisobutyrylation	ELDAIGTKRFDSEKA CCCCCCCCCCCCCCC	45.94	-
294	Ubiquitination	ELDAIGTKRFDSEKA CCCCCCCCCCCCCCC	45.94	21890473
300	Acetylation	TKRFDSEKAGDREVQ CCCCCCCCCCCHHHH	62.72	25953088
300	Ubiquitination	TKRFDSEKAGDREVQ CCCCCCCCCCCHHHH	62.72	21890473
310	Sulfoxidation	DREVQRTMLELLNQL CHHHHHHHHHHHHHC	2.74	28183972
327	Ubiquitination	FQPNTQVKVIAATNR CCCCCEEEEEEECCC	20.36	21890473
332	Phosphorylation	QVKVIAATNRVDILD EEEEEEECCCCCCCC	17.97	20068231
345	Phosphorylation	LDPALLRSGRLDRKI CCHHHHHCCCCCCEE	28.38	-
351	Ubiquitination	RSGRLDRKIEFPMPN HCCCCCCEEECCCCC	46.37	-
356	Sulfoxidation	DRKIEFPMPNEEARA CCEEECCCCCHHHHH	7.27	21406390
370	Phosphorylation	ARIMQIHSRKMNVSP HHHHHHHHCCCCCCC	34.91	21406692
372	Ubiquitination	IMQIHSRKMNVSPDV HHHHHHCCCCCCCCC	37.53	21890473
373	Sulfoxidation	MQIHSRKMNVSPDVN HHHHHCCCCCCCCCC	6.10	30846556
376	Phosphorylation	HSRKMNVSPDVNYEE HHCCCCCCCCCCHHH	15.46	25159151
381	Phosphorylation	NVSPDVNYEELARCT CCCCCCCHHHHHHCC	15.61	21406692
388	Phosphorylation	YEELARCTDDFNGAQ HHHHHHCCCCCCCCC	32.81	21406692
397	Ubiquitination	DFNGAQCKAVCVEAG CCCCCCCEEEHHHHH	31.60	-
400	Glutathionylation	GAQCKAVCVEAGMIA CCCCEEEHHHHHHHH	2.46	22555962
405	Sulfoxidation	AVCVEAGMIALRRGA EEHHHHHHHHHHCCC	1.77	21406390
420	Phosphorylation	TELTHEDYMEGILEV CCCCHHHHHHHHHHH	8.29	-
421	Sulfoxidation	ELTHEDYMEGILEVQ CCCHHHHHHHHHHHH	6.18	30846556
431	Ubiquitination	ILEVQAKKKANLQYY HHHHHHHHHCCCCCC	61.20	-
432	Ubiquitination	LEVQAKKKANLQYYA HHHHHHHHCCCCCCC	41.63	-
437	Phosphorylation	KKKANLQYYA----- HHHCCCCCCC-----	12.43	29496907
438	Phosphorylation	KKANLQYYA------ HHCCCCCCC------	7.90	29496907

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 PRS6A_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PRS6A_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 PRS6A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
VHL_HUMAN	VHL	physical	14556007
HIF1A_HUMAN	HIF1A	physical	14556007
EPAS1_HUMAN	EPAS1	physical	14556007
TRXR2_HUMAN	TXNRD2	physical	11463857
PRS8_HUMAN	PSMC5	physical	11463857
CDN2A_HUMAN	CDKN2A	physical	17334400
ARF_HUMAN	CDKN2A	physical	17334400
MDM2_HUMAN	MDM2	physical	20479273
P53_HUMAN	TP53	physical	20479273
C2TA_HUMAN	CIITA	physical	20351748
PRS6A_HUMAN	PSMC3	physical	21675959
PRS8_HUMAN	PSMC5	physical	20810900
PAAF1_HUMAN	PAAF1	physical	15831487
PRS4_HUMAN	PSMC1	physical	21628461
PSMD8_HUMAN	PSMD8	physical	21628461
PSB5_HUMAN	PSMB5	physical	21628461
PSMD6_HUMAN	PSMD6	physical	22275368
PSMD8_HUMAN	PSMD8	physical	22275368
PSMD2_HUMAN	PSMD2	physical	22275368
PSMD1_HUMAN	PSMD1	physical	22275368
PRS7_HUMAN	PSMC2	physical	22275368
PRS4_HUMAN	PSMC1	physical	22275368
PRS10_HUMAN	PSMC6	physical	22275368
PRS6B_HUMAN	PSMC4	physical	22275368
PRS8_HUMAN	PSMC5	physical	22275368
FOSL1_HUMAN	FOSL1	physical	21874050
STAT1_HUMAN	STAT1	physical	19853614
HOP2_HUMAN	PSMC3IP	physical	19325002
ANDR_HUMAN	AR	physical	19325002
CDN2A_HUMAN	CDKN2A	physical	14665636
ARF_HUMAN	CDKN2A	physical	14665636
SYN2_HUMAN	SYN2	physical	11032911
PRS6A_HUMAN	PSMC3	physical	8419915
PRS8_HUMAN	PSMC5	physical	22939629
PRS6B_HUMAN	PSMC4	physical	22939629
PSD13_HUMAN	PSMD13	physical	22939629
PSMD7_HUMAN	PSMD7	physical	22939629
PSMD6_HUMAN	PSMD6	physical	22939629
PSD10_HUMAN	PSMD10	physical	22939629
PRS7_HUMAN	PSMC2	physical	22939629
PSD11_HUMAN	PSMD11	physical	22939629
PSD12_HUMAN	PSMD12	physical	22939629
PSMD1_HUMAN	PSMD1	physical	22939629
PSMD2_HUMAN	PSMD2	physical	22939629
PSMD3_HUMAN	PSMD3	physical	22939629
PSMD4_HUMAN	PSMD4	physical	22939629
PSMD8_HUMAN	PSMD8	physical	22939629
PSDE_HUMAN	PSMD14	physical	22939629
PSA2_HUMAN	PSMA2	physical	22939629
PSA5_HUMAN	PSMA5	physical	22939629
PSA6_HUMAN	PSMA6	physical	22939629
PSA7_HUMAN	PSMA7	physical	22939629
PSB7_HUMAN	PSMB7	physical	22939629
PSB1_HUMAN	PSMB1	physical	22939629
PSA3_HUMAN	PSMA3	physical	22939629
PSB5_HUMAN	PSMB5	physical	22939629
PSA1_HUMAN	PSMA1	physical	22939629
PSB3_HUMAN	PSMB3	physical	22939629
PSB4_HUMAN	PSMB4	physical	22939629
PSB2_HUMAN	PSMB2	physical	22939629
PSB6_HUMAN	PSMB6	physical	22939629
UBP14_HUMAN	USP14	physical	22939629
PSB8_HUMAN	PSMB8	physical	22939629
PSA7L_HUMAN	PSMA8	physical	22939629
UBFD1_HUMAN	UBFD1	physical	22939629
RANB9_HUMAN	RANBP9	physical	22939629
ZFY16_HUMAN	ZFYVE16	physical	22939629
RUVB1_HUMAN	RUVBL1	physical	22939629
ECD_HUMAN	ECD	physical	22939629
STIP1_HUMAN	STIP1	physical	22939629
ADRM1_HUMAN	ADRM1	physical	22863883
PRS4_HUMAN	PSMC1	physical	22863883
PRS7_HUMAN	PSMC2	physical	22863883
PRS6B_HUMAN	PSMC4	physical	22863883
PRS10_HUMAN	PSMC6	physical	22863883
PSDE_HUMAN	PSMD14	physical	22863883
PSMD1_HUMAN	PSMD1	physical	22863883
PSMD3_HUMAN	PSMD3	physical	22863883
UCHL5_HUMAN	UCHL5	physical	22863883
PRS6A_HUMAN	PSMC3	physical	25416956
PRS10_HUMAN	PSMC6	physical	25416956
PSMD9_HUMAN	PSMD9	physical	25416956
KDM1A_HUMAN	KDM1A	physical	25416956
AMOL2_HUMAN	AMOTL2	physical	25416956
PSA2_BOVIN	PSMA2	physical	24770418
UBC_HUMAN	UBC	physical	24743594
PSMD1_HUMAN	PSMD1	physical	26186194
IF4G1_HUMAN	EIF4G1	physical	26186194
IF4G3_HUMAN	EIF4G3	physical	26186194
RAI14_HUMAN	RAI14	physical	26186194
CSR2B_HUMAN	CSRP2BP	physical	26186194
ZZZ3_HUMAN	ZZZ3	physical	26186194
PRS6B_HUMAN	PSMC4	physical	26186194
PRS8_HUMAN	PSMC5	physical	26186194
YETS2_HUMAN	YEATS2	physical	26186194
KIF1A_HUMAN	KIF1A	physical	26186194
KIF1B_HUMAN	KIF1B	physical	26186194
FWCH2_HUMAN	FLYWCH2	physical	26186194
PSD11_HUMAN	PSMD11	physical	26186194
PRS10_HUMAN	PSMC6	physical	26186194
PSMD2_HUMAN	PSMD2	physical	26186194
NFRKB_HUMAN	NFRKB	physical	26186194
PSD10_HUMAN	PSMD10	physical	26186194
TPD53_HUMAN	TPD52L1	physical	26186194
FBX28_HUMAN	FBXO28	physical	26186194
F117B_HUMAN	FAM117B	physical	26186194
LIN54_HUMAN	LIN54	physical	26186194
RL23_HUMAN	RPL23	physical	26186194
PSD12_HUMAN	PSMD12	physical	26186194
LRIF1_HUMAN	LRIF1	physical	26186194
MGAP_HUMAN	MGA	physical	26186194
PSMD6_HUMAN	PSMD6	physical	26186194
MBIP1_HUMAN	MBIP	physical	26186194
T2FA_HUMAN	GTF2F1	physical	26186194
MPRIP_HUMAN	MPRIP	physical	26186194
TBD2B_HUMAN	TBC1D2B	physical	26186194
SLMAP_HUMAN	SLMAP	physical	26186194
CHD8_HUMAN	CHD8	physical	26186194
PARD3_HUMAN	PARD3	physical	26186194
NC2B_HUMAN	DR1	physical	26186194
TAD2A_HUMAN	TADA2A	physical	26186194
GARS_HUMAN	GARS	physical	26186194
TRAF4_HUMAN	TRAF4	physical	26186194
PININ_HUMAN	PNN	physical	26186194
EIF2D_HUMAN	EIF2D	physical	26186194
DIAP1_HUMAN	DIAPH1	physical	26186194
RING2_HUMAN	RNF2	physical	26186194
ITPR2_HUMAN	ITPR2	physical	26186194
LMBL2_HUMAN	L3MBTL2	physical	26186194
WNK2_HUMAN	WNK2	physical	26186194
STKL1_HUMAN	STKLD1	physical	26186194
PEX6_HUMAN	PEX6	physical	26186194
ELF2_HUMAN	ELF2	physical	26186194
PMS1_HUMAN	PMS1	physical	26186194
SEN15_HUMAN	TSEN15	physical	26186194
NEDD1_HUMAN	NEDD1	physical	26186194
SPAS2_HUMAN	SPATS2	physical	26186194
FA83D_HUMAN	FAM83D	physical	26186194
KXDL1_HUMAN	KXD1	physical	26186194
A16L1_HUMAN	ATG16L1	physical	26186194
MAVS_HUMAN	MAVS	physical	26186194
UBXN1_HUMAN	UBXN1	physical	26186194
RNH2C_HUMAN	RNASEH2C	physical	26186194
TSR3_HUMAN	TSR3	physical	26186194
ARHG1_HUMAN	ARHGEF1	physical	26186194
E2F6_HUMAN	E2F6	physical	26186194
CXXC1_HUMAN	CXXC1	physical	26186194
M3K7_HUMAN	MAP3K7	physical	26186194
TRMO_HUMAN	C9orf156	physical	26186194
ADRM1_HUMAN	ADRM1	physical	26344197
BASP1_HUMAN	BASP1	physical	26344197
NAA15_HUMAN	NAA15	physical	26344197
PHB2_HUMAN	PHB2	physical	26344197
PSA1_HUMAN	PSMA1	physical	26344197
PSA2_HUMAN	PSMA2	physical	26344197
PSA4_HUMAN	PSMA4	physical	26344197
PSB2_HUMAN	PSMB2	physical	26344197
PSB4_HUMAN	PSMB4	physical	26344197
PSB5_HUMAN	PSMB5	physical	26344197
PSB8_HUMAN	PSMB8	physical	26344197
PRS8_HUMAN	PSMC5	physical	26344197
PSD11_HUMAN	PSMD11	physical	26344197
PSD12_HUMAN	PSMD12	physical	26344197
PSD13_HUMAN	PSMD13	physical	26344197
PSDE_HUMAN	PSMD14	physical	26344197
PSMD2_HUMAN	PSMD2	physical	26344197
PSMD7_HUMAN	PSMD7	physical	26344197
PSMD8_HUMAN	PSMD8	physical	26344197
PSMG2_HUMAN	PSMG2	physical	26344197
RFC2_HUMAN	RFC2	physical	26344197
RPN1_HUMAN	RPN1	physical	26344197
TRAF4_HUMAN	TRAF4	physical	28514442
EIF2D_HUMAN	EIF2D	physical	28514442
ELF2_HUMAN	ELF2	physical	28514442
RAI14_HUMAN	RAI14	physical	28514442
MPRIP_HUMAN	MPRIP	physical	28514442
RNH2C_HUMAN	RNASEH2C	physical	28514442
FBX28_HUMAN	FBXO28	physical	28514442
PSD10_HUMAN	PSMD10	physical	28514442
F117B_HUMAN	FAM117B	physical	28514442
PEX6_HUMAN	PEX6	physical	28514442
CHD8_HUMAN	CHD8	physical	28514442
ZZZ3_HUMAN	ZZZ3	physical	28514442
PARD3_HUMAN	PARD3	physical	28514442
ARHG1_HUMAN	ARHGEF1	physical	28514442
PSD12_HUMAN	PSMD12	physical	28514442
STKL1_HUMAN	STKLD1	physical	28514442
MBIP1_HUMAN	MBIP	physical	28514442
NFRKB_HUMAN	NFRKB	physical	28514442
PHF19_HUMAN	PHF19	physical	28514442
KXDL1_HUMAN	KXD1	physical	28514442
YETS2_HUMAN	YEATS2	physical	28514442
CSR2B_HUMAN	CSRP2BP	physical	28514442
TPD53_HUMAN	TPD52L1	physical	28514442
PSMD1_HUMAN	PSMD1	physical	28514442
LMBL2_HUMAN	L3MBTL2	physical	28514442
KIF1A_HUMAN	KIF1A	physical	28514442
TBD2B_HUMAN	TBC1D2B	physical	28514442
TAD2A_HUMAN	TADA2A	physical	28514442
LRIF1_HUMAN	LRIF1	physical	28514442
FA83D_HUMAN	FAM83D	physical	28514442
LIN54_HUMAN	LIN54	physical	28514442
PRS6B_HUMAN	PSMC4	physical	28514442
TRMO_HUMAN	C9orf156	physical	28514442
E2F6_HUMAN	E2F6	physical	28514442
PRS10_HUMAN	PSMC6	physical	28514442
GARS_HUMAN	GARS	physical	28514442
SPAS2_HUMAN	SPATS2	physical	28514442
UBXN1_HUMAN	UBXN1	physical	28514442
A16L1_HUMAN	ATG16L1	physical	28514442
SCML1_HUMAN	SCML1	physical	28514442
M3K7_HUMAN	MAP3K7	physical	28514442
T2FA_HUMAN	GTF2F1	physical	28514442
MGAP_HUMAN	MGA	physical	28514442
RL23_HUMAN	RPL23	physical	28514442
NEDD1_HUMAN	NEDD1	physical	28514442
CXXC1_HUMAN	CXXC1	physical	28514442
SLMAP_HUMAN	SLMAP	physical	28514442
PSMD2_HUMAN	PSMD2	physical	28514442
TAB1_HUMAN	TAB1	physical	28514442
TSR3_HUMAN	TSR3	physical	28514442
FWCH2_HUMAN	FLYWCH2	physical	28514442
KIF1B_HUMAN	KIF1B	physical	28514442
SEN15_HUMAN	TSEN15	physical	28514442
MAVS_HUMAN	MAVS	physical	28514442
MARK4_HUMAN	MARK4	physical	28514442
E2AK4_HUMAN	EIF2AK4	physical	28514442
PSMD6_HUMAN	PSMD6	physical	28514442
MEX3D_HUMAN	MEX3D	physical	28514442
INTU_HUMAN	INTU	physical	27173435

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.

Regulatory Network of PRS6A_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-9, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Mass spectrometric characterization of the affinity-purified human26S proteasome complex."; Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.; Biochemistry 46:3553-3565(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, ACETYLATION AT MET-1,AND MASS SPECTROMETRY.	17323924 [Abstract]
Phosphorylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-9, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Mass spectrometric characterization of the affinity-purified human26S proteasome complex."; Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.; Biochemistry 46:3553-3565(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, ACETYLATION AT MET-1,AND MASS SPECTROMETRY.	17323924 [Abstract]