HSP72_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HSP72_HUMAN
• UniProt AC: P54652
• Protein Name: Heat shock-related 70 kDa protein 2
• Gene Name: HSPA2
• Organism: Homo sapiens (Human).
• Sequence Length: 639
• Subcellular Localization: Cytoplasm, cytoskeleton, spindle . Colocalizes with SHCBP1L at spindle during the meiosis process.
• Protein Description: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. [PubMed: 26865365 Plays a role in spermatogenesis. In association with SHCBP1L may participate in the maintenance of spindle integrity during meiosis in male germ cells (By similarity]
• Protein Sequence: MSARGPAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDATVQSDMKHWPFRVVSEGGKPKVQVEYKGETKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAGTITGLNVLRIINEPTAAAIAYGLDKKGCAGGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSHLAEEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGVDFYTSITRARFEELNADLFRGTLEPVEKALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILIGDKSENVQDLLLLDVTPLSLGIETAGGVMTPLIKRNTTIPTKQTQTFTTYSDNQSSVLVQVYEGERAMTKDNNLLGKFDLTGIPPAPRGVPQIEVTFDIDANGILNVTAADKSTGKENKITITNDKGRLSKDDIDRMVQEAERYKSEDEANRDRVAAKNALESYTYNIKQTVEDEKLRGKISEQDKNKILDKCQEVINWLDRNQMAEKDEYEHKQKELERVCNPIISKLYQGGPGGGSGGGGSGASGGPTIEEVD

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
14	Phosphorylation	AIGIDLGTTYSCVGV EEEEECCCCEEEEEE	29.83	26714015
15	Phosphorylation	IGIDLGTTYSCVGVF EEEECCCCEEEEEEE	16.19	26714015
16	Phosphorylation	GIDLGTTYSCVGVFQ EEECCCCEEEEEEEE	10.42	26714015
17	Phosphorylation	IDLGTTYSCVGVFQH EECCCCEEEEEEEEC	10.55	26714015
26	Ubiquitination	VGVFQHGKVEIIAND EEEEECCEEEEEECC	34.27	-
38	Phosphorylation	ANDQGNRTTPSYVAF ECCCCCCCCCCEEEE	47.24	21945579
39	Phosphorylation	NDQGNRTTPSYVAFT CCCCCCCCCCEEEEE	13.65	21945579
41	Phosphorylation	QGNRTTPSYVAFTDT CCCCCCCCEEEEECH	30.10	21945579
42	Phosphorylation	GNRTTPSYVAFTDTE CCCCCCCEEEEECHH	9.30	21945579
46	Phosphorylation	TPSYVAFTDTERLIG CCCEEEEECHHHHHH	32.07	21945579
48	Phosphorylation	SYVAFTDTERLIGDA CEEEEECHHHHHHHH	21.68	21945579
50	Methylation	VAFTDTERLIGDAAK EEEECHHHHHHHHHH	33.43	-
57	Acetylation	RLIGDAAKNQVAMNP HHHHHHHHCCCCCCC	50.02	66723797
65	Phosphorylation	NQVAMNPTNTIFDAK CCCCCCCCCCHHHHH	39.73	-
67	Phosphorylation	VAMNPTNTIFDAKRL CCCCCCCCHHHHHHH	26.04	-
72	Acetylation	TNTIFDAKRLIGRKF CCCHHHHHHHHCCCC	49.97	7822225
78	Ubiquitination	AKRLIGRKFEDATVQ HHHHHCCCCCCCCCC	48.14	-
88	Sulfoxidation	DATVQSDMKHWPFRV CCCCCCCCCCCCEEE	4.10	30846556
89	Acetylation	ATVQSDMKHWPFRVV CCCCCCCCCCCEEEE	47.73	25038526
101	Ubiquitination	RVVSEGGKPKVQVEY EEEEECCCCEEEEEE	53.15	-
103	Ubiquitination	VSEGGKPKVQVEYKG EEECCCCEEEEEECC	49.11	-
108	Phosphorylation	KPKVQVEYKGETKTF CCEEEEEECCCEEEE	25.99	20090780
109	Acetylation	PKVQVEYKGETKTFF CEEEEEECCCEEEEC	36.44	11924973
109	Ubiquitination	PKVQVEYKGETKTFF CEEEEEECCCEEEEC	36.44	21890473
112	Phosphorylation	QVEYKGETKTFFPEE EEEECCCEEEECHHH	44.01	28152594
113	Acetylation	VEYKGETKTFFPEEI EEECCCEEEECHHHH	38.75	25038526
113	Ubiquitination	VEYKGETKTFFPEEI EEECCCEEEECHHHH	38.75	-
114	Phosphorylation	EYKGETKTFFPEEIS EECCCEEEECHHHHH	37.62	23663014
121	Phosphorylation	TFFPEEISSMVLTKM EECHHHHHHHHHHHH	18.70	23663014
122	Phosphorylation	FFPEEISSMVLTKMK ECHHHHHHHHHHHHH	20.69	23663014
126	Phosphorylation	EISSMVLTKMKEIAE HHHHHHHHHHHHHHH	20.06	23663014
129	Acetylation	SMVLTKMKEIAEAYL HHHHHHHHHHHHHHH	47.74	25038526
135	Phosphorylation	MKEIAEAYLGGKVHS HHHHHHHHHCCCCEE	9.44	29396449
139	Acetylation	AEAYLGGKVHSAVIT HHHHHCCCCEEEEEE	34.67	25038526
142	Phosphorylation	YLGGKVHSAVITVPA HHCCCCEEEEEEEEC	27.50	30624053
146	Phosphorylation	KVHSAVITVPAYFND CCEEEEEEEECCCCH	17.53	25693802
150	Phosphorylation	AVITVPAYFNDSQRQ EEEEEECCCCHHHCC	9.24	-
154	Phosphorylation	VPAYFNDSQRQATKD EECCCCHHHCCCCCC	28.50	17525332
159	Phosphorylation	NDSQRQATKDAGTIT CHHHCCCCCCCCCCC	22.56	-
164	Phosphorylation	QATKDAGTITGLNVL CCCCCCCCCCCCCHH	19.65	21406692
166	Phosphorylation	TKDAGTITGLNVLRI CCCCCCCCCCCHHEE	35.14	21406692
178	Phosphorylation	LRIINEPTAAAIAYG HEECCCCHHHHHHHC	23.81	28152594
184	Phosphorylation	PTAAAIAYGLDKKGC CHHHHHHHCCCCCCC	16.47	28152594
188	Acetylation	AIAYGLDKKGCAGGE HHHHCCCCCCCCCCC	56.99	11923469
188	Ubiquitination	AIAYGLDKKGCAGGE HHHHCCCCCCCCCCC	56.99	21890473
189	Ubiquitination	IAYGLDKKGCAGGEK HHHCCCCCCCCCCCC	59.91	-
223	Ubiquitination	EDGIFEVKSTAGDTH CCCEEEEEECCCCCC	34.59	-
224	Phosphorylation	DGIFEVKSTAGDTHL CCEEEEEECCCCCCC	28.76	25850435
225	Phosphorylation	GIFEVKSTAGDTHLG CEEEEEECCCCCCCC	29.01	25850435
229	Phosphorylation	VKSTAGDTHLGGEDF EEECCCCCCCCCCCC	20.34	26329039
249	Acetylation	SHLAEEFKRKHKKDI HHHHHHHHHHHHHCC	64.91	25038526
268	Phosphorylation	RAVRRLRTACERAKR HHHHHHHHHHHHHHH	40.01	27273156
276	Phosphorylation	ACERAKRTLSSSTQA HHHHHHHHHCCCCCE	30.22	-
280	Phosphorylation	AKRTLSSSTQASIEI HHHHHCCCCCEEEEH	22.59	22817900
299	Phosphorylation	EGVDFYTSITRARFE CCCCCHHHHHHHHHH	15.58	20860994
301	Phosphorylation	VDFYTSITRARFEEL CCCHHHHHHHHHHHH	20.31	20860994
322	Acetylation	GTLEPVEKALRDAKL CCCHHHHHHHHHCCC	53.61	37092745
328	Ubiquitination	EKALRDAKLDKGQIQ HHHHHHCCCCCCCCC	62.60	21890473
343	Phosphorylation	EIVLVGGSTRIPKIQ EEEEECCCCCHHHHH	14.48	-
344	Phosphorylation	IVLVGGSTRIPKIQK EEEECCCCCHHHHHH	35.57	28985074
348	Ubiquitination	GGSTRIPKIQKLLQD CCCCCHHHHHHHHHH	56.23	-
351	Acetylation	TRIPKIQKLLQDFFN CCHHHHHHHHHHHHC	55.42	22640839
351	Ubiquitination	TRIPKIQKLLQDFFN CCHHHHHHHHHHHHC	55.42	21890473
360	Acetylation	LQDFFNGKELNKSIN HHHHHCCCCCCCCCC	61.20	72584811
360	Sumoylation	LQDFFNGKELNKSIN HHHHHCCCCCCCCCC	61.20	-
360	Ubiquitination	LQDFFNGKELNKSIN HHHHHCCCCCCCCCC	61.20	21890473
364	Sumoylation	FNGKELNKSINPDEA HCCCCCCCCCCHHHH	66.39	-
364	Ubiquitination	FNGKELNKSINPDEA HCCCCCCCCCCHHHH	66.39	-
365	Phosphorylation	NGKELNKSINPDEAV CCCCCCCCCCHHHHH	26.90	25159151
374	Phosphorylation	NPDEAVAYGAAVQAA CHHHHHHHHHHHHHH	10.74	18669648
400	Phosphorylation	DLLLLDVTPLSLGIE HEEEEECCCCCCCEE	20.41	20068231
403	Phosphorylation	LLDVTPLSLGIETAG EEECCCCCCCEEECC	26.25	22817900
408	Phosphorylation	PLSLGIETAGGVMTP CCCCCEEECCCCCCC	28.78	27251275
414	Phosphorylation	ETAGGVMTPLIKRNT EECCCCCCCEEECCC	16.73	24719451
421	Phosphorylation	TPLIKRNTTIPTKQT CCEEECCCCCCCCCC	30.09	26437602
422	Phosphorylation	PLIKRNTTIPTKQTQ CEEECCCCCCCCCCE	28.63	27251275
428	Phosphorylation	TTIPTKQTQTFTTYS CCCCCCCCEEEEEEC	31.00	25693802
430	Phosphorylation	IPTKQTQTFTTYSDN CCCCCCEEEEEECCC	26.74	25693802
432	Phosphorylation	TKQTQTFTTYSDNQS CCCCEEEEEECCCCC	28.36	21601212
433	Phosphorylation	KQTQTFTTYSDNQSS CCCEEEEEECCCCCE	19.48	21601212
434	Phosphorylation	QTQTFTTYSDNQSSV CCEEEEEECCCCCEE	15.80	25693802
435	Phosphorylation	TQTFTTYSDNQSSVL CEEEEEECCCCCEEE	28.17	25693802
439	Phosphorylation	TTYSDNQSSVLVQVY EEECCCCCEEEEEEE	28.77	25693802
440	Phosphorylation	TYSDNQSSVLVQVYE EECCCCCEEEEEEEE	15.09	25693802
453	Phosphorylation	YEGERAMTKDNNLLG EECCCCCCCCCCCCC	33.97	22210691
454	Acetylation	EGERAMTKDNNLLGK ECCCCCCCCCCCCCC	45.43	66696417
454	Ubiquitination	EGERAMTKDNNLLGK ECCCCCCCCCCCCCC	45.43	21890473
465	Phosphorylation	LLGKFDLTGIPPAPR CCCCCCCCCCCCCCC	34.60	21406692
472	Methylation	TGIPPAPRGVPQIEV CCCCCCCCCCCEEEE	61.93	80701957
480	Phosphorylation	GVPQIEVTFDIDANG CCCEEEEEEEECCCC	11.64	22817900
498	Phosphorylation	VTAADKSTGKENKIT EEEECCCCCCCCCEE	59.00	-
500	Ubiquitination	AADKSTGKENKITIT EECCCCCCCCCEEEE	59.19	-
503	Ubiquitination	KSTGKENKITITNDK CCCCCCCCEEEECCC	42.17	21890473
505	Phosphorylation	TGKENKITITNDKGR CCCCCCEEEECCCCC	24.29	25159151
507	Phosphorylation	KENKITITNDKGRLS CCCCEEEECCCCCCC	28.81	21601212
510	Sumoylation	KITITNDKGRLSKDD CEEEECCCCCCCHHH	48.26	-
510	Acetylation	KITITNDKGRLSKDD CEEEECCCCCCCHHH	48.26	72617499
510	Sumoylation	KITITNDKGRLSKDD CEEEECCCCCCCHHH	48.26	-
510	Ubiquitination	KITITNDKGRLSKDD CEEEECCCCCCCHHH	48.26	21890473
514	Phosphorylation	TNDKGRLSKDDIDRM ECCCCCCCHHHHHHH	32.45	30622161
515	Acetylation	NDKGRLSKDDIDRMV CCCCCCCHHHHHHHH	65.10	12439133
520	Dimethylation	LSKDDIDRMVQEAER CCHHHHHHHHHHHHH	27.75	-
520	Methylation	LSKDDIDRMVQEAER CCHHHHHHHHHHHHH	27.75	115372595
527	Dimethylation	RMVQEAERYKSEDEA HHHHHHHHHHCCCHH	51.75	-
527	Methylation	RMVQEAERYKSEDEA HHHHHHHHHHCCCHH	51.75	115372601
530	Phosphorylation	QEAERYKSEDEANRD HHHHHHHCCCHHHHH	41.15	30622161
564	"N6,N6,N6-trimethyllysine"	EDEKLRGKISEQDKN CCHHHCCCCCHHHHH	36.30	-
564	Methylation	EDEKLRGKISEQDKN CCHHHCCCCCHHHHH	36.30	23921388
566	Phosphorylation	EKLRGKISEQDKNKI HHHCCCCCHHHHHHH	32.46	21601212
589	Sulfoxidation	NWLDRNQMAEKDEYE HHHCHHHHHCHHHHH	6.25	30846556
614	Phosphorylation	NPIISKLYQGGPGGG HHHHHHHHCCCCCCC	14.62	25693802
622	Phosphorylation	QGGPGGGSGGGGSGA CCCCCCCCCCCCCCC	37.22	30622161
627	Phosphorylation	GGSGGGGSGASGGPT CCCCCCCCCCCCCCC	34.17	28348404
630	Phosphorylation	GGGGSGASGGPTIEE CCCCCCCCCCCCCCC	48.05	28348404
634	Phosphorylation	SGASGGPTIEEVD-- CCCCCCCCCCCCC--	44.27	25693802

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of HSP72_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of HSP72_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of HSP72_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HPBP1_HUMAN	HSPBP1	physical	16189514
EWS_HUMAN	EWSR1	physical	16713569
HPBP1_HUMAN	HSPBP1	physical	16713569
MEOX2_HUMAN	MEOX2	physical	16713569
A4_HUMAN	APP	physical	21832049
HSP7C_HUMAN	HSPA8	physical	22939629
TRI38_HUMAN	TRIM38	physical	25416956
HPBP1_HUMAN	HSPBP1	physical	25416956
STIP1_HUMAN	STIP1	physical	26344197
BAG6_HUMAN	BAG6	physical	26153132

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-42 AND TYR-108, AND MASSSPECTROMETRY.
PubMed: 18083107