dbPTM

HPBP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HPBP1_HUMAN
UniProt AC	Q9NZL4
Protein Name	Hsp70-binding protein 1
Gene Name	HSPBP1
Organism	Homo sapiens (Human).
Sequence Length	362
Subcellular Localization
Protein Description	Inhibits HSPA1A chaperone activity by changing the conformation of the ATP-binding domain of HSPA1A and interfering with ATP binding. Interferes with ubiquitination mediated by STUB1 and inhibits chaperone-assisted degradation of immature CFTR..
Protein Sequence	MSDEGSRGSRLPLALPPASQGCSSGGGGGGGGGSSAGGSGNSRPPRNLQGLLQMAITAGSEEPDPPPEPMSEERRQWLQEAMSAAFRGQREEVEQMKSCLRVLSQPMPPTAGEAEQAADQQEREGALELLADLCENMDNAADFCQLSGMHLLVGRYLEAGAAGLRWRAAQLIGTCSQNVAAIQEQVLGLGALRKLLRLLDRDACDTVRVKALFAISCLVREQEAGLLQFLRLDGFSVLMRAMQQQVQKLKVKSAFLLQNLLVGHPEHKGTLCSMGMVQQLVALVRTEHSPFHEHVLGALCSLVTDFPQGVRECREPELGLEELLRHRCQLLQQHEEYQEELEFCEKLLQTCFSSPADDSMDR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSDEGSRGS ------CCCCCCCCC	44.35	22210691
9	Phosphorylation	SDEGSRGSRLPLALP CCCCCCCCCCCCCCC	29.54	-
19	Phosphorylation	PLALPPASQGCSSGG CCCCCCHHHCCCCCC	32.64	22210691
24	Phosphorylation	PASQGCSSGGGGGGG CHHHCCCCCCCCCCC	45.60	28555341
34	Phosphorylation	GGGGGGGSSAGGSGN CCCCCCCCCCCCCCC	21.93	21712546
35	Phosphorylation	GGGGGGSSAGGSGNS CCCCCCCCCCCCCCC	33.92	22210691
36	Phosphorylation	GGGGGSSAGGSGNSR CCCCCCCCCCCCCCC	28.23	-
39	Phosphorylation	GGSSAGGSGNSRPPR CCCCCCCCCCCCCCC	33.61	21712546
42	Phosphorylation	SAGGSGNSRPPRNLQ CCCCCCCCCCCCCHH	50.09	28555341
54	Phosphorylation	NLQGLLQMAITAGSE CHHHHHHHHHHCCCC	2.69	27251275
57	Phosphorylation	GLLQMAITAGSEEPD HHHHHHHHCCCCCCC	18.54	28348404
60	Phosphorylation	QMAITAGSEEPDPPP HHHHHCCCCCCCCCC	36.00	28348404
83	Phosphorylation	QWLQEAMSAAFRGQR HHHHHHHHHHHHCCH	24.40	-
94	Ubiquitination	RGQREEVEQMKSCLR HCCHHHHHHHHHHHH	48.51	27667366
97	Acetylation	REEVEQMKSCLRVLS HHHHHHHHHHHHHHC	37.40	25953088
97	Ubiquitination	REEVEQMKSCLRVLS HHHHHHHHHHHHHHC	37.40	-
107	Sulfoxidation	LRVLSQPMPPTAGEA HHHHCCCCCCCCCHH	4.87	21406390
140	Ubiquitination	LCENMDNAADFCQLS HHHCCCCHHHHHHHH	12.25	27667366
156	Phosphorylation	MHLLVGRYLEAGAAG HHHHHHHHHHHHHHH	11.72	20068231
162	Methylation	RYLEAGAAGLRWRAA HHHHHHHHHHHHHHH	19.35	-
165	Methylation	EAGAAGLRWRAAQLI HHHHHHHHHHHHHHH	21.66	115479993
206	Phosphorylation	LDRDACDTVRVKALF HCCCCCHHHHHHHHH	15.31	-
207	Ubiquitination	DRDACDTVRVKALFA CCCCCHHHHHHHHHH	4.18	33845483
210	Ubiquitination	ACDTVRVKALFAISC CCHHHHHHHHHHHHH	28.89	-
233	Phosphorylation	LLQFLRLDGFSVLMR HHHHHHCCHHHHHHH	50.05	-
236	Phosphorylation	FLRLDGFSVLMRAMQ HHHCCHHHHHHHHHH	21.63	21406692
239	Sulfoxidation	LDGFSVLMRAMQQQV CCHHHHHHHHHHHHH	2.11	21406390
245	Ubiquitination	LMRAMQQQVQKLKVK HHHHHHHHHHHHHHH	23.79	21890473
248	Malonylation	AMQQQVQKLKVKSAF HHHHHHHHHHHHHHH	51.96	26320211
248	Acetylation	AMQQQVQKLKVKSAF HHHHHHHHHHHHHHH	51.96	25953088
248	Ubiquitination	AMQQQVQKLKVKSAF HHHHHHHHHHHHHHH	51.96	21890473
249	Ubiquitination	MQQQVQKLKVKSAFL HHHHHHHHHHHHHHH	4.27	-
250	Ubiquitination	QQQVQKLKVKSAFLL HHHHHHHHHHHHHHH	55.44	-
253	Ubiquitination	VQKLKVKSAFLLQNL HHHHHHHHHHHHHHH	27.52	33845483
291 (in isoform 1)	Ubiquitination	-	13.64	21890473
291	Ubiquitination	VRTEHSPFHEHVLGA HHCCCCHHHHHHHHH	13.64	21890473
291	Ubiquitination	VRTEHSPFHEHVLGA HHCCCCHHHHHHHHH	13.64	21890473
350	Phosphorylation	FCEKLLQTCFSSPAD HHHHHHHHHHCCCCC	18.58	30266825
351	Phosphorylation	CEKLLQTCFSSPADD HHHHHHHHHCCCCCC	1.69	20068231
353	Phosphorylation	KLLQTCFSSPADDSM HHHHHHHCCCCCCCC	37.24	23401153
354	Phosphorylation	LLQTCFSSPADDSMD HHHHHHCCCCCCCCC	12.12	29255136
356	Phosphorylation	QTCFSSPADDSMDR- HHHHCCCCCCCCCC-	34.88	20068231
359	Phosphorylation	FSSPADDSMDR---- HCCCCCCCCCC----	24.11	20201521
359	Methylation	FSSPADDSMDR---- HCCCCCCCCCC----	24.11	-
362	Methylation	PADDSMDR------- CCCCCCCC-------	39.54	115479985

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 HPBP1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of HPBP1_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 HPBP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HSP7C_HUMAN	HSPA8	physical	16169070
LRIF1_HUMAN	LRIF1	physical	16169070
CHIP_HUMAN	STUB1	physical	15215316
HSP7C_RAT	Hspa8	physical	15215316
HSP7C_HUMAN	HSPA8	physical	15215316
PGRP1_HUMAN	PGLYRP1	physical	21247889
A4_HUMAN	APP	physical	21832049
HSP74_HUMAN	HSPA4	physical	19659607
GRP75_HUMAN	HSPA9	physical	19659607
GRP78_HUMAN	HSPA5	physical	19659607
OGT1_HUMAN	OGT	physical	22863883
SHLB1_HUMAN	SH3GLB1	physical	22863883
TM1L1_HUMAN	TOM1L1	physical	22863883
WDR4_HUMAN	WDR4	physical	22863883
ZPR1_HUMAN	ZPR1	physical	22863883
NT2NL_HUMAN	NOTCH2NL	physical	25416956
HSP7C_HUMAN	HSPA8	physical	26186194
HSP76_HUMAN	HSPA6	physical	26186194
EDRF1_HUMAN	EDRF1	physical	26186194
5NTC_HUMAN	NT5C2	physical	26186194
ELF2_HUMAN	ELF2	physical	26186194
ARP2_HUMAN	ACTR2	physical	26344197
NMD3_HUMAN	NMD3	physical	26344197
5NTC_HUMAN	NT5C2	physical	28514442
EDRF1_HUMAN	EDRF1	physical	28514442
ELF2_HUMAN	ELF2	physical	28514442
HSF1_HUMAN	HSF1	physical	28514442
CF106_HUMAN	C6orf106	physical	28514442
ABL2_HUMAN	ABL2	physical	28514442
CLH2_HUMAN	CLTCL1	physical	28514442
HSF2_HUMAN	HSF2	physical	28514442
ZN703_HUMAN	ZNF703	physical	28514442
GAK_HUMAN	GAK	physical	28514442
TACC3_HUMAN	TACC3	physical	28514442
UBAP2_HUMAN	UBAP2	physical	28514442
DJC13_HUMAN	DNAJC13	physical	28514442
HGS_HUMAN	HGS	physical	28514442
FOXC1_HUMAN	FOXC1	physical	28514442
SF01_HUMAN	SF1	physical	28514442
M3K7_HUMAN	MAP3K7	physical	28514442
TAB1_HUMAN	TAB1	physical	28514442
DPH2_HUMAN	DPH2	physical	28514442
HSP72_HUMAN	HSPA2	physical	28514442
QSER1_HUMAN	QSER1	physical	28514442
RUFY1_HUMAN	RUFY1	physical	28514442
ARFP1_HUMAN	ARFIP1	physical	28514442
QRIC1_HUMAN	QRICH1	physical	28514442
NEDD1_HUMAN	NEDD1	physical	28514442
ZN503_HUMAN	ZNF503	physical	28514442
SF3A3_HUMAN	SF3A3	physical	28514442
HSP76_HUMAN	HSPA6	physical	28514442
HSF1_HUMAN	HSF1	physical	27173435
MKLN1_HUMAN	MKLN1	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 HPBP1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354 AND SER-359, ANDMASS SPECTROMETRY.	18669648 [Abstract]