dbPTM

AHSA1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AHSA1_HUMAN
UniProt AC	O95433
Protein Name	Activator of 90 kDa heat shock protein ATPase homolog 1
Gene Name	AHSA1
Organism	Homo sapiens (Human).
Sequence Length	338
Subcellular Localization	Cytoplasm, cytosol . Endoplasmic reticulum . May transiently interact with the endoplasmic reticulum.
Protein Description	Acts as a co-chaperone of HSP90AA1. [PubMed: 29127155 Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity]
Protein Sequence	MAKWGEGDPRWIVEERADATNVNNWHWTERDASNWSTDKLKTLFLAVQVQNEEGKCEVTEVSKLDGEASINNRKGKLIFFYEWSVKLNWTGTSKSGVQYKGHVEIPNLSDENSVDEVEISVSLAKDEPDTNLVALMKEEGVKLLREAMGIYISTLKTEFTQGMILPTMNGESVDPVGQPALKTEERKAKPAPSKTQARPVGVKIPTCKITLKETFLTSPEELYRVFTTQELVQAFTHAPATLEADRGGKFHMVDGNVSGEFTDLVPEKHIVMKWRFKSWPEGHFATITLTFIDKNGETELCMEGRGIPAPEEERTRQGWQRYYFEGIKQTFGYGARLF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Methylation	-----MAKWGEGDPR -----CCCCCCCCCC	55.20	19608861
3	Acetylation	-----MAKWGEGDPR -----CCCCCCCCCC	55.20	-
3	Ubiquitination	-----MAKWGEGDPR -----CCCCCCCCCC	55.20	19608861
3	Ubiquitination	-----MAKWGEGDPR -----CCCCCCCCCC	55.20	-
3	Acetylation	-----MAKWGEGDPR -----CCCCCCCCCC	55.20	19608861
30	Methylation	NNWHWTERDASNWST CCCCCCCCCCCCCCH	37.10	-
36	Phosphorylation	ERDASNWSTDKLKTL CCCCCCCCHHHHHHE	30.86	20873877
37	Phosphorylation	RDASNWSTDKLKTLF CCCCCCCHHHHHHEE	28.86	20873877
39	Acetylation	ASNWSTDKLKTLFLA CCCCCHHHHHHEEEE	52.55	26822725
39	Ubiquitination	ASNWSTDKLKTLFLA CCCCCHHHHHHEEEE	52.55	-
69	Phosphorylation	SKLDGEASINNRKGK EECCCEEEECCCCCE	22.88	20873877
94	Ubiquitination	LNWTGTSKSGVQYKG EECCCCCCCCCEEEE	51.58	21890473
94	Acetylation	LNWTGTSKSGVQYKG EECCCCCCCCCEEEE	51.58	27452117
94	Ubiquitination	LNWTGTSKSGVQYKG EECCCCCCCCCEEEE	51.58	21890473
94	Ubiquitination	LNWTGTSKSGVQYKG EECCCCCCCCCEEEE	51.58	21890473
95	Phosphorylation	NWTGTSKSGVQYKGH ECCCCCCCCCEEEEE	43.92	22210691
99	Phosphorylation	TSKSGVQYKGHVEIP CCCCCCEEEEEEECC	19.28	22210691
109	Phosphorylation	HVEIPNLSDENSVDE EEECCCCCCCCCCCE	49.90	20068231
113	Phosphorylation	PNLSDENSVDEVEIS CCCCCCCCCCEEEEE	28.97	20068231
120	Phosphorylation	SVDEVEISVSLAKDE CCCEEEEEEEEECCC	7.67	20068231
122	Phosphorylation	DEVEISVSLAKDEPD CEEEEEEEEECCCCC	18.80	20068231
130	Phosphorylation	LAKDEPDTNLVALMK EECCCCCCCHHHHHH	40.96	20068231
136	Sulfoxidation	DTNLVALMKEEGVKL CCCHHHHHHHHHHHH	3.56	21406390
137	Ubiquitination	TNLVALMKEEGVKLL CCHHHHHHHHHHHHH	54.16	-
137	2-Hydroxyisobutyrylation	TNLVALMKEEGVKLL CCHHHHHHHHHHHHH	54.16	-
142	Acetylation	LMKEEGVKLLREAMG HHHHHHHHHHHHHHC	53.30	25953088
151	Phosphorylation	LREAMGIYISTLKTE HHHHHCCHHHCCCCC	5.31	110738293
153	Phosphorylation	EAMGIYISTLKTEFT HHHCCHHHCCCCCCC	15.66	20068231
154	Phosphorylation	AMGIYISTLKTEFTQ HHCCHHHCCCCCCCC	23.79	20068231
163	Sulfoxidation	KTEFTQGMILPTMNG CCCCCCCCEEECCCC	1.73	21406390
167	Phosphorylation	TQGMILPTMNGESVD CCCCEEECCCCCCCC	21.59	27251275
168	Sulfoxidation	QGMILPTMNGESVDP CCCEEECCCCCCCCC	5.99	28183972
172	Phosphorylation	LPTMNGESVDPVGQP EECCCCCCCCCCCCC	32.97	28348404
182	Sumoylation	PVGQPALKTEERKAK CCCCCCCCCCHHCCC	56.87	25114211
183	Phosphorylation	VGQPALKTEERKAKP CCCCCCCCCHHCCCC	43.88	72243471
193	Phosphorylation	RKAKPAPSKTQARPV HCCCCCCCCCCCCCC	50.90	24300666
194	Acetylation	KAKPAPSKTQARPVG CCCCCCCCCCCCCCC	43.53	25953088
194	Ubiquitination	KAKPAPSKTQARPVG CCCCCCCCCCCCCCC	43.53	-
203	Ubiquitination	QARPVGVKIPTCKIT CCCCCCCCCCCCEEE	36.72	-
203	Ubiquitination	QARPVGVKIPTCKIT CCCCCCCCCCCCEEE	36.72	-
203	Acetylation	QARPVGVKIPTCKIT CCCCCCCCCCCCEEE	36.72	25953088
203	Sumoylation	QARPVGVKIPTCKIT CCCCCCCCCCCCEEE	36.72	28112733
207	S-nitrosocysteine	VGVKIPTCKITLKET CCCCCCCCEEEEEEE	2.23	-
207	S-nitrosylation	VGVKIPTCKITLKET CCCCCCCCEEEEEEE	2.23	19483679
208	Ubiquitination	GVKIPTCKITLKETF CCCCCCCEEEEEEEE	41.00	-
208	Ubiquitination	GVKIPTCKITLKETF CCCCCCCEEEEEEEE	41.00	-
208	Malonylation	GVKIPTCKITLKETF CCCCCCCEEEEEEEE	41.00	26320211
208	Acetylation	GVKIPTCKITLKETF CCCCCCCEEEEEEEE	41.00	25953088
210	Phosphorylation	KIPTCKITLKETFLT CCCCCEEEEEEEECC	19.78	24719451
212	Ubiquitination	PTCKITLKETFLTSP CCCEEEEEEEECCCH	46.16	21890473
212	Ubiquitination	PTCKITLKETFLTSP CCCEEEEEEEECCCH	46.16	21890473
212	Malonylation	PTCKITLKETFLTSP CCCEEEEEEEECCCH	46.16	26320211
212	Acetylation	PTCKITLKETFLTSP CCCEEEEEEEECCCH	46.16	19608861
212	Ubiquitination	PTCKITLKETFLTSP CCCEEEEEEEECCCH	46.16	21890473
212	Acetylation	PTCKITLKETFLTSP CCCEEEEEEEECCCH	46.16	-
214	Phosphorylation	CKITLKETFLTSPEE CEEEEEEEECCCHHH	23.51	36012977
217	Phosphorylation	TLKETFLTSPEELYR EEEEEECCCHHHHHH	37.74	26356563
218	Phosphorylation	LKETFLTSPEELYRV EEEEECCCHHHHHHH	32.25	28348404
223	Phosphorylation	LTSPEELYRVFTTQE CCCHHHHHHHHCHHH	14.17	26356563
241	Phosphorylation	AFTHAPATLEADRGG HHCCCCCEEEECCCC	24.87	46160873
249	Ubiquitination	LEADRGGKFHMVDGN EEECCCCCEEEECCC	34.61	21890473
249	Ubiquitination	LEADRGGKFHMVDGN EEECCCCCEEEECCC	34.61	21890473
249	Acetylation	LEADRGGKFHMVDGN EEECCCCCEEEECCC	34.61	-
249	Ubiquitination	LEADRGGKFHMVDGN EEECCCCCEEEECCC	34.61	21890473
249	Acetylation	LEADRGGKFHMVDGN EEECCCCCEEEECCC	34.61	23954790
258	Phosphorylation	HMVDGNVSGEFTDLV EEECCCCCCCCCCCC	36.28	30266825
262	Phosphorylation	GNVSGEFTDLVPEKH CCCCCCCCCCCCCCE	24.91	30266825
268	Ubiquitination	FTDLVPEKHIVMKWR CCCCCCCCEEEEEEE	32.34	-
273	Acetylation	PEKHIVMKWRFKSWP CCCEEEEEEECCCCC	25.07	25953088
278	Phosphorylation	VMKWRFKSWPEGHFA EEEEECCCCCCCCEE	45.19	28258704
298	Phosphorylation	FIDKNGETELCMEGR EECCCCCEEEEECCC	35.34	28258704
305	Methylation	TELCMEGRGIPAPEE EEEEECCCCCCCCHH	26.93	-
321	Methylation	RTRQGWQRYYFEGIK HHHHHHHHHHHHHHH	22.93	-
322	Phosphorylation	TRQGWQRYYFEGIKQ HHHHHHHHHHHHHHH	9.45	28152594
323	Phosphorylation	RQGWQRYYFEGIKQT HHHHHHHHHHHHHHH	9.42	28152594
328	Ubiquitination	RYYFEGIKQTFGYGA HHHHHHHHHHHCCCC	54.89	21890473
328	Ubiquitination	RYYFEGIKQTFGYGA HHHHHHHHHHHCCCC	54.89	21890473
328	Ubiquitination	RYYFEGIKQTFGYGA HHHHHHHHHHHCCCC	54.89	21890473
333	Phosphorylation	GIKQTFGYGARLF-- HHHHHHCCCCCCC--	11.92	28152594
336	Methylation	QTFGYGARLF----- HHHCCCCCCC-----	32.06	-

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
223	Y	Phosphorylation	Kinase	ABL1	P00519	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of AHSA1_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 AHSA1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
DNJB4_HUMAN	DNAJB4	physical	22939629
DX39A_HUMAN	DDX39A	physical	22863883
IF4H_HUMAN	EIF4H	physical	22863883
PSF2_HUMAN	GINS2	physical	22863883
GSHR_HUMAN	GSR	physical	22863883
6PGD_HUMAN	PGD	physical	22863883
PPP5_HUMAN	PPP5C	physical	25036637
HS90B_HUMAN	HSP90AB1	physical	25036637
FKBP5_HUMAN	FKBP5	physical	25036637
HS90A_HUMAN	HSP90AA1	physical	25036637
FKBP4_HUMAN	FKBP4	physical	25036637
PPID_HUMAN	PPID	physical	25036637
CHRD1_HUMAN	CHORDC1	physical	25036637
TOM34_HUMAN	TOMM34	physical	25036637
SYTM_HUMAN	TARS2	physical	25036637
ACADM_HUMAN	ACADM	physical	26344197
ASNS_HUMAN	ASNS	physical	26344197
ATPG_HUMAN	ATP5C1	physical	26344197
TCPZ_HUMAN	CCT6A	physical	26344197
TCPW_HUMAN	CCT6B	physical	26344197
DX39A_HUMAN	DDX39A	physical	26344197
DX39B_HUMAN	DDX39B	physical	26344197
DNJA4_HUMAN	DNAJA4	physical	26344197
DNJB4_HUMAN	DNAJB4	physical	26344197
SYEP_HUMAN	EPRS	physical	26344197
GALE_HUMAN	GALE	physical	26344197
GFPT1_HUMAN	GFPT1	physical	26344197
GFPT2_HUMAN	GFPT2	physical	26344197
DHB12_HUMAN	HSD17B12	physical	26344197
CH10_HUMAN	HSPE1	physical	26344197
SYIC_HUMAN	IARS	physical	26344197
IDH3G_HUMAN	IDH3G	physical	26344197
IMA3_HUMAN	KPNA4	physical	26344197
LDHB_HUMAN	LDHB	physical	26344197
NMD3_HUMAN	NMD3	physical	26344197
RAB1A_HUMAN	RAB1A	physical	26344197
RAB1B_HUMAN	RAB1B	physical	26344197
RD23B_HUMAN	RAD23B	physical	26344197
SEC13_HUMAN	SEC13	physical	26344197
STAT1_HUMAN	STAT1	physical	26344197
STIP1_HUMAN	STIP1	physical	26344197
UBA1_HUMAN	UBA1	physical	26344197
ZYX_HUMAN	ZYX	physical	26344197
RL23_HUMAN	RPL23	physical	26693507
RL17_HUMAN	RPL17	physical	26693507
RS3A_HUMAN	RPS3A	physical	26693507
PRP31_HUMAN	PRPF31	physical	26693507
TCPB_HUMAN	CCT2	physical	26693507
PAIRB_HUMAN	SERBP1	physical	26693507
EIF3G_HUMAN	EIF3G	physical	26693507
RBMX_HUMAN	RBMX	physical	26693507
DDX3X_HUMAN	DDX3X	physical	26693507
TCPD_HUMAN	CCT4	physical	26693507
IF4B_HUMAN	EIF4B	physical	26693507
SFPQ_HUMAN	SFPQ	physical	26693507
UBIM_HUMAN	FAU	physical	26693507
ENOA_HUMAN	ENO1	physical	26693507
RS14_HUMAN	RPS14	physical	26693507
ALDOA_HUMAN	ALDOA	physical	26693507
RL31_HUMAN	RPL31	physical	26693507
TR150_HUMAN	THRAP3	physical	26693507
RS3_HUMAN	RPS3	physical	26693507
FAS_HUMAN	FASN	physical	26693507
ROA1_HUMAN	HNRNPA1	physical	26693507
HNRPU_HUMAN	HNRNPU	physical	26693507
LDHA_HUMAN	LDHA	physical	26693507
RS15A_HUMAN	RPS15A	physical	26693507
EF1A1_HUMAN	EEF1A1	physical	26693507
RS23_HUMAN	RPS23	physical	26693507
MCM7_HUMAN	MCM7	physical	26693507
RS4X_HUMAN	RPS4X	physical	26693507
GRP78_HUMAN	HSPA5	physical	26693507
ACLY_HUMAN	ACLY	physical	26693507
RBM10_HUMAN	RBM10	physical	26693507
RS20_HUMAN	RPS20	physical	26693507
RS2_HUMAN	RPS2	physical	26693507
ADT3_HUMAN	SLC25A6	physical	26693507
RS7_HUMAN	RPS7	physical	26693507
ANM5_HUMAN	PRMT5	physical	26693507
TBB2A_HUMAN	TUBB2A	physical	26693507
EIF3L_HUMAN	EIF3L	physical	26693507
RS15_HUMAN	RPS15	physical	26693507
RL11_HUMAN	RPL11	physical	26693507
RS18_HUMAN	RPS18	physical	26693507
RL9_HUMAN	RPL9	physical	26693507
RS13_HUMAN	RPS13	physical	26693507
HS90A_HUMAN	HSP90AA1	physical	26693507
HNRH1_HUMAN	HNRNPH1	physical	26693507
TCPQ_HUMAN	CCT8	physical	26693507
HSP7C_HUMAN	HSPA8	physical	26693507
RS10_HUMAN	RPS10	physical	26693507
CIRBP_HUMAN	CIRBP	physical	26693507
CH60_HUMAN	HSPD1	physical	26693507
EIF3A_HUMAN	EIF3A	physical	26693507
RL22_HUMAN	RPL22	physical	26693507
EIF3B_HUMAN	EIF3B	physical	26693507
LDHB_HUMAN	LDHB	physical	26693507
VIME_HUMAN	VIM	physical	26693507
IMB1_HUMAN	KPNB1	physical	26693507
RS16_HUMAN	RPS16	physical	26693507
HS90B_HUMAN	HSP90AB1	physical	26693507
TIF1B_HUMAN	TRIM28	physical	26693507
RS11_HUMAN	RPS11	physical	26693507
U5S1_HUMAN	EFTUD2	physical	26693507
RS25_HUMAN	RPS25	physical	26693507
ROA2_HUMAN	HNRNPA2B1	physical	26693507
BCLF1_HUMAN	BCLAF1	physical	26693507
RBM39_HUMAN	RBM39	physical	26693507
IMDH2_HUMAN	IMPDH2	physical	26693507
DCD_HUMAN	DCD	physical	26693507
MCM2_HUMAN	MCM2	physical	26693507
TFR1_HUMAN	TFRC	physical	26693507
PSMD3_HUMAN	PSMD3	physical	26693507
RL13_HUMAN	RPL13	physical	26693507
LS14A_HUMAN	LSM14A	physical	26693507
RL38_HUMAN	RPL38	physical	26693507
PSMD2_HUMAN	PSMD2	physical	26693507
HNRPK_HUMAN	HNRNPK	physical	26693507
GDE_HUMAN	AGL	physical	26693507
TCPG_HUMAN	CCT3	physical	26693507
PRDX6_HUMAN	PRDX6	physical	26693507
AT1A1_HUMAN	ATP1A1	physical	26693507
P121A_HUMAN	POM121	physical	26693507
UFL1_HUMAN	UFL1	physical	26693507
UBF1_HUMAN	UBTF	physical	26693507
PLK1_HUMAN	PLK1	physical	26693507
RL6_HUMAN	RPL6	physical	26693507
CKAP5_HUMAN	CKAP5	physical	26693507
DPOD3_HUMAN	POLD3	physical	26693507
ZCCHV_HUMAN	ZC3HAV1	physical	26693507
TF3C2_HUMAN	GTF3C2	physical	26693507
CKAP2_HUMAN	CKAP2	physical	26693507
ARHG1_HUMAN	ARHGEF1	physical	26693507
UHRF1_HUMAN	UHRF1	physical	26693507
PRP19_HUMAN	PRPF19	physical	26693507
MYH2_HUMAN	MYH2	physical	26693507
HS90A_HUMAN	HSP90AA1	physical	22504172
TEBP_HUMAN	PTGES3	physical	22504172
DNJA1_HUMAN	DNAJA1	physical	22504172
HSP7C_HUMAN	HSPA8	physical	22504172
AKT1_HUMAN	AKT1	physical	22504172
PKN2_HUMAN	PKN2	physical	22504172
SRPK1_HUMAN	SRPK1	physical	22504172
PPM1G_HUMAN	PPM1G	physical	22504172
PRKDC_HUMAN	PRKDC	physical	22504172
IQGA1_HUMAN	IQGAP1	physical	22504172
TOP2A_HUMAN	TOP2A	physical	22504172
XRCC5_HUMAN	XRCC5	physical	22504172
XRCC6_HUMAN	XRCC6	physical	22504172
RACK1_HUMAN	GNB2L1	physical	22504172
HS90A_HUMAN	HSP90AA1	physical	27353360

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 AHSA1_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-3 AND LYS-212, AND MASSSPECTROMETRY.	19608861 [Abstract]