HSP7C_HUMAN - dbPTM
HSP7C_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HSP7C_HUMAN
UniProt AC P11142
Protein Name Heat shock cognate 71 kDa protein
Gene Name HSPA8
Organism Homo sapiens (Human).
Sequence Length 646
Subcellular Localization Cytoplasm. Melanosome. Nucleus, nucleolus. Cell membrane. Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock.
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. [PubMed: 21150129]
Protein Sequence MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVEDEKLQGKINDEDKQKILDKCNEIINWLDKNQTAEKEEFEHQQKELEKVCNPIITKLYQSAGGMPGGMPGGFPGGGAPPSGGASSGPTIEEVD
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 Orthologous
Protein Cluster
2Acetylation------MSKGPAVGI
------CCCCCEEEE
46.4419413330
2Phosphorylation------MSKGPAVGI
------CCCCCEEEE
46.4423401153
2 (in isoform 2)Acetylation-46.44-
3Acetylation-----MSKGPAVGID
-----CCCCCEEEEE
68.5623236377
3Ubiquitination-----MSKGPAVGID
-----CCCCCEEEEE
68.5621890473
13PhosphorylationAVGIDLGTTYSCVGV
EEEEECCCCEEEEEE
29.8328152594
14PhosphorylationVGIDLGTTYSCVGVF
EEEECCCCEEEEEEE
16.1928464451
15PhosphorylationGIDLGTTYSCVGVFQ
EEECCCCEEEEEEEE
10.4228152594
16PhosphorylationIDLGTTYSCVGVFQH
EECCCCEEEEEEEEC
10.5528152594
17GlutathionylationDLGTTYSCVGVFQHG
ECCCCEEEEEEEECC
1.8622555962
17S-palmitoylationDLGTTYSCVGVFQHG
ECCCCEEEEEEEECC
1.8629575903
25UbiquitinationVGVFQHGKVEIIAND
EEEEECCEEEEEECC
34.27-
37PhosphorylationANDQGNRTTPSYVAF
ECCCCCCCCCCEEEE
47.2421945579
38PhosphorylationNDQGNRTTPSYVAFT
CCCCCCCCCCEEEEE
13.6521945579
40PhosphorylationQGNRTTPSYVAFTDT
CCCCCCCCEEEEECH
30.1021945579
41NitrationGNRTTPSYVAFTDTE
CCCCCCCEEEEECHH
9.30-
41PhosphorylationGNRTTPSYVAFTDTE
CCCCCCCEEEEECHH
9.3021945579
45PhosphorylationTPSYVAFTDTERLIG
CCCEEEEECHHHHHH
32.0721945579
47PhosphorylationSYVAFTDTERLIGDA
CEEEEECHHHHHHHH
21.6821945579
49MethylationVAFTDTERLIGDAAK
EEEECHHHHHHHHHH
33.43-
56AcetylationRLIGDAAKNQVAMNP
HHHHHHHHCCCCCCC
50.0223954790
56MalonylationRLIGDAAKNQVAMNP
HHHHHHHHCCCCCCC
50.0226320211
56UbiquitinationRLIGDAAKNQVAMNP
HHHHHHHHCCCCCCC
50.0221890473
56 (in isoform 1)Ubiquitination-50.0221890473
56 (in isoform 2)Ubiquitination-50.0221890473
61SulfoxidationAAKNQVAMNPTNTVF
HHHCCCCCCCCCCHH
6.9228465586
64PhosphorylationNQVAMNPTNTVFDAK
CCCCCCCCCCHHHHH
38.2223911959
66PhosphorylationVAMNPTNTVFDAKRL
CCCCCCCCHHHHHHH
25.6522817900
71AcetylationTNTVFDAKRLIGRRF
CCCHHHHHHHHCCCC
49.9725825284
71SuccinylationTNTVFDAKRLIGRRF
CCCHHHHHHHHCCCC
49.9723954790
71UbiquitinationTNTVFDAKRLIGRRF
CCCHHHHHHHHCCCC
49.9721890473
71 (in isoform 1)Ubiquitination-49.9721890473
71 (in isoform 2)Ubiquitination-49.9721890473
85PhosphorylationFDDAVVQSDMKHWPF
CCCHHHCCCCCCCCE
28.2330266825
87SulfoxidationDAVVQSDMKHWPFMV
CHHHCCCCCCCCEEE
4.1021406390
88TrimethylationAVVQSDMKHWPFMVV
HHHCCCCCCCCEEEE
47.73-
88AcetylationAVVQSDMKHWPFMVV
HHHCCCCCCCCEEEE
47.7321466224
88MethylationAVVQSDMKHWPFMVV
HHHCCCCCCCCEEEE
47.73-
88UbiquitinationAVVQSDMKHWPFMVV
HHHCCCCCCCCEEEE
47.7321890473
88 (in isoform 1)Ubiquitination-47.7321890473
88 (in isoform 2)Acetylation-47.73-
88 (in isoform 2)Ubiquitination-47.7321890473
93SulfoxidationDMKHWPFMVVNDAGR
CCCCCCEEEECCCCC
2.6330846556
102UbiquitinationVNDAGRPKVQVEYKG
ECCCCCCEEEEEECC
43.89-
107PhosphorylationRPKVQVEYKGETKSF
CCEEEEEECCCEECC
25.9920090780
108AcetylationPKVQVEYKGETKSFY
CEEEEEECCCEECCC
36.4423749302
108MalonylationPKVQVEYKGETKSFY
CEEEEEECCCEECCC
36.4426320211
108UbiquitinationPKVQVEYKGETKSFY
CEEEEEECCCEECCC
36.4419608861
108 (in isoform 1)Ubiquitination-36.4421890473
108 (in isoform 2)Acetylation-36.44-
108 (in isoform 2)Ubiquitination-36.4421890473
111PhosphorylationQVEYKGETKSFYPEE
EEEECCCEECCCHHH
40.4328152594
112AcetylationVEYKGETKSFYPEEV
EEECCCEECCCHHHH
33.9823954790
112UbiquitinationVEYKGETKSFYPEEV
EEECCCEECCCHHHH
33.9821890473
112 (in isoform 1)Ubiquitination-33.9821890473
112 (in isoform 2)Ubiquitination-33.9821890473
113PhosphorylationEYKGETKSFYPEEVS
EECCCEECCCHHHHH
37.1221712546
115NitrationKGETKSFYPEEVSSM
CCCEECCCHHHHHHH
19.47-
115PhosphorylationKGETKSFYPEEVSSM
CCCEECCCHHHHHHH
19.4728152594
120PhosphorylationSFYPEEVSSMVLTKM
CCCHHHHHHHHHHHH
18.9228152594
121PhosphorylationFYPEEVSSMVLTKMK
CCHHHHHHHHHHHHH
20.3428152594
122SulfoxidationYPEEVSSMVLTKMKE
CHHHHHHHHHHHHHH
1.9230846556
125PhosphorylationEVSSMVLTKMKEIAE
HHHHHHHHHHHHHHH
20.0628152594
126AcetylationVSSMVLTKMKEIAEA
HHHHHHHHHHHHHHH
43.7625953088
126UbiquitinationVSSMVLTKMKEIAEA
HHHHHHHHHHHHHHH
43.7621890473
126 (in isoform 1)Ubiquitination-43.7621890473
126 (in isoform 2)Ubiquitination-43.7621890473
127SulfoxidationSSMVLTKMKEIAEAY
HHHHHHHHHHHHHHH
3.8721406390
128AcetylationSMVLTKMKEIAEAYL
HHHHHHHHHHHHHHC
47.7472627929
128UbiquitinationSMVLTKMKEIAEAYL
HHHHHHHHHHHHHHC
47.7421906983
128 (in isoform 1)Ubiquitination-47.7421890473
128 (in isoform 2)Ubiquitination-47.7421890473
134PhosphorylationMKEIAEAYLGKTVTN
HHHHHHHHCCCCCCC
13.9028152594
137AcetylationIAEAYLGKTVTNAVV
HHHHHCCCCCCCEEE
36.9123954790
137UbiquitinationIAEAYLGKTVTNAVV
HHHHHCCCCCCCEEE
36.9121890473
137 (in isoform 1)Ubiquitination-36.9121890473
137 (in isoform 2)Acetylation-36.91-
137 (in isoform 2)Ubiquitination-36.9121890473
138PhosphorylationAEAYLGKTVTNAVVT
HHHHCCCCCCCEEEE
30.6628152594
140PhosphorylationAYLGKTVTNAVVTVP
HHCCCCCCCEEEEEE
23.7728152594
145PhosphorylationTVTNAVVTVPAYFND
CCCCEEEEEECCCCH
17.7428152594
149PhosphorylationAVVTVPAYFNDSQRQ
EEEEEECCCCHHHCC
9.2428152594
153PhosphorylationVPAYFNDSQRQATKD
EECCCCHHHCCHHCC
28.5017525332
153 (in isoform 2)Phosphorylation-28.50-
158PhosphorylationNDSQRQATKDAGTIA
CHHHCCHHCCCCCCC
22.5625159151
159AcetylationDSQRQATKDAGTIAG
HHHCCHHCCCCCCCC
48.9023749302
159MalonylationDSQRQATKDAGTIAG
HHHCCHHCCCCCCCC
48.9026320211
159UbiquitinationDSQRQATKDAGTIAG
HHHCCHHCCCCCCCC
48.9021890473
159 (in isoform 1)Ubiquitination-48.9021890473
159 (in isoform 2)Ubiquitination-48.9021890473
163PhosphorylationQATKDAGTIAGLNVL
CHHCCCCCCCCCHHH
14.9023911959
177PhosphorylationLRIINEPTAAAIAYG
HHHCCCHHHHHHHHC
23.8128152594
183NitrationPTAAAIAYGLDKKVG
HHHHHHHHCCCCCCC
16.47-
183PhosphorylationPTAAAIAYGLDKKVG
HHHHHHHHCCCCCCC
16.4728152594
187AcetylationAIAYGLDKKVGAERN
HHHHCCCCCCCCCCC
55.1723954790
187MalonylationAIAYGLDKKVGAERN
HHHHCCCCCCCCCCC
55.1726320211
187UbiquitinationAIAYGLDKKVGAERN
HHHHCCCCCCCCCCC
55.1721890473
187 (in isoform 1)Ubiquitination-55.1721890473
187 (in isoform 2)Ubiquitination-55.1721890473
188UbiquitinationIAYGLDKKVGAERNV
HHHCCCCCCCCCCCE
45.6422053931
188 (in isoform 1)Ubiquitination-45.6421890473
188 (in isoform 2)Ubiquitination-45.6421890473
220UbiquitinationEDGIFEVKSTAGDTH
CCCEEEEEECCCCCC
34.59-
221PhosphorylationDGIFEVKSTAGDTHL
CCEEEEEECCCCCCC
28.7625850435
222PhosphorylationGIFEVKSTAGDTHLG
CEEEEEECCCCCCCC
29.0125850435
226PhosphorylationVKSTAGDTHLGGEDF
EEECCCCCCCCCCCC
20.3426329039
237SulfoxidationGEDFDNRMVNHFIAE
CCCCCHHHHHHHHHH
4.4230846556
246AcetylationNHFIAEFKRKHKKDI
HHHHHHHHHHHHCCC
52.6319608861
246MalonylationNHFIAEFKRKHKKDI
HHHHHHHHHHHHCCC
52.6326320211
246MethylationNHFIAEFKRKHKKDI
HHHHHHHHHHHHCCC
52.6319608861
246UbiquitinationNHFIAEFKRKHKKDI
HHHHHHHHHHHHCCC
52.6321890473
246 (in isoform 1)Ubiquitination-52.6321890473
246 (in isoform 2)Acetylation-52.63-
246 (in isoform 2)Ubiquitination-52.6321890473
248UbiquitinationFIAEFKRKHKKDISE
HHHHHHHHHHCCCHH
61.44-
251UbiquitinationEFKRKHKKDISENKR
HHHHHHHCCCHHHHH
61.0721906983
251 (in isoform 1)Ubiquitination-61.0721890473
251 (in isoform 2)Ubiquitination-61.0721890473
254PhosphorylationRKHKKDISENKRAVR
HHHHCCCHHHHHHHH
45.2926055452
254 (in isoform 2)Phosphorylation-45.29-
257AcetylationKKDISENKRAVRRLR
HCCCHHHHHHHHHHH
37.3723749302
257SumoylationKKDISENKRAVRRLR
HCCCHHHHHHHHHHH
37.37-
257UbiquitinationKKDISENKRAVRRLR
HCCCHHHHHHHHHHH
37.3721890473
257 (in isoform 1)Ubiquitination-37.3721890473
257 (in isoform 2)Ubiquitination-37.3721890473
265PhosphorylationRAVRRLRTACERAKR
HHHHHHHHHHHHHHH
40.0127273156
273PhosphorylationACERAKRTLSSSTQA
HHHHHHHHHCCCCCE
30.22-
277PhosphorylationAKRTLSSSTQASIEI
HHHHHCCCCCEEEEH
22.5922817900
296PhosphorylationEGIDFYTSITRARFE
CCCCHHHHHHHHHHH
15.5820860994
298PhosphorylationIDFYTSITRARFEEL
CCHHHHHHHHHHHHH
20.3120860994
313PhosphorylationNADLFRGTLDPVEKA
CHHHHCCCCCHHHHH
24.5922817900
319AcetylationGTLDPVEKALRDAKL
CCCCHHHHHHHHCCC
53.6119608861
319MalonylationGTLDPVEKALRDAKL
CCCCHHHHHHHHCCC
53.6126320211
319SuccinylationGTLDPVEKALRDAKL
CCCCHHHHHHHHCCC
53.61-
319SuccinylationGTLDPVEKALRDAKL
CCCCHHHHHHHHCCC
53.61-
319UbiquitinationGTLDPVEKALRDAKL
CCCCHHHHHHHHCCC
53.6121890473
319 (in isoform 1)Ubiquitination-53.6121890473
319 (in isoform 2)Acetylation-53.61-
319 (in isoform 2)Ubiquitination-53.6121890473
325AcetylationEKALRDAKLDKSQIH
HHHHHHCCCCHHHCC
62.6025953088
325MalonylationEKALRDAKLDKSQIH
HHHHHHCCCCHHHCC
62.6026320211
325UbiquitinationEKALRDAKLDKSQIH
HHHHHHCCCCHHHCC
62.60-
325 (in isoform 1)Ubiquitination-62.6021890473
325 (in isoform 2)Ubiquitination-62.6021890473
328AcetylationLRDAKLDKSQIHDIV
HHHCCCCHHHCCEEE
55.4823954790
328MalonylationLRDAKLDKSQIHDIV
HHHCCCCHHHCCEEE
55.4826320211
328UbiquitinationLRDAKLDKSQIHDIV
HHHCCCCHHHCCEEE
55.4821890473
328 (in isoform 1)Ubiquitination-55.4821890473
328 (in isoform 2)Ubiquitination-55.4821890473
329PhosphorylationRDAKLDKSQIHDIVL
HHCCCCHHHCCEEEE
33.7526055452
329 (in isoform 2)Phosphorylation-33.75-
340PhosphorylationDIVLVGGSTRIPKIQ
EEEEECCCCCCHHHH
14.4820873877
341PhosphorylationIVLVGGSTRIPKIQK
EEEECCCCCCHHHHH
35.5720873877
345UbiquitinationGGSTRIPKIQKLLQD
CCCCCCHHHHHHHHH
56.23-
348AcetylationTRIPKIQKLLQDFFN
CCCHHHHHHHHHHHC
55.4223954790
348SuccinylationTRIPKIQKLLQDFFN
CCCHHHHHHHHHHHC
55.4223954790
348UbiquitinationTRIPKIQKLLQDFFN
CCCHHHHHHHHHHHC
55.4221890473
348 (in isoform 1)Ubiquitination-55.4221890473
348 (in isoform 2)Acetylation-55.42-
348 (in isoform 2)Ubiquitination-55.4221890473
357AcetylationLQDFFNGKELNKSIN
HHHHHCCCCCCCCCC
61.2023749302
357SuccinylationLQDFFNGKELNKSIN
HHHHHCCCCCCCCCC
61.2023954790
357SumoylationLQDFFNGKELNKSIN
HHHHHCCCCCCCCCC
61.20-
357UbiquitinationLQDFFNGKELNKSIN
HHHHHCCCCCCCCCC
61.2021890473
357 (in isoform 1)Ubiquitination-61.2021890473
357 (in isoform 2)Ubiquitination-61.2021890473
361AcetylationFNGKELNKSINPDEA
HCCCCCCCCCCHHHH
66.3923954790
361SumoylationFNGKELNKSINPDEA
HCCCCCCCCCCHHHH
66.39-
361UbiquitinationFNGKELNKSINPDEA
HCCCCCCCCCCHHHH
66.3921890473
361 (in isoform 1)Ubiquitination-66.3921890473
361 (in isoform 2)Ubiquitination-66.3921890473
362PhosphorylationNGKELNKSINPDEAV
CCCCCCCCCCHHHHH
26.9030278072
362 (in isoform 2)Phosphorylation-26.90-
371NitrationNPDEAVAYGAAVQAA
CHHHHHHHHHHHHHH
10.74-
371PhosphorylationNPDEAVAYGAAVQAA
CHHHHHHHHHHHHHH
10.7418669648
381PhosphorylationAVQAAILSGDKSENV
HHHHHHHCCCCCCCH
38.5419060867
385PhosphorylationAILSGDKSENVQDLL
HHHCCCCCCCHHHEE
38.8620068231
385 (in isoform 2)Phosphorylation-38.86-
397PhosphorylationDLLLLDVTPLSLGIE
HEEEEECCCCCCCCE
20.4120068231
397 (in isoform 2)Phosphorylation-20.41-
400PhosphorylationLLDVTPLSLGIETAG
EEECCCCCCCCEECC
26.2520068231
405PhosphorylationPLSLGIETAGGVMTV
CCCCCCEECCCEEEE
28.7820068231
411PhosphorylationETAGGVMTVLIKRNT
EECCCEEEEEEECCC
15.1120068231
415UbiquitinationGVMTVLIKRNTTIPT
CEEEEEEECCCCCCC
35.12-
418PhosphorylationTVLIKRNTTIPTKQT
EEEEECCCCCCCCEE
30.0926437602
419PhosphorylationVLIKRNTTIPTKQTQ
EEEECCCCCCCCEEE
28.6327251275
423UbiquitinationRNTTIPTKQTQTFTT
CCCCCCCCEEEEEEE
46.0922053931
423 (in isoform 1)Ubiquitination-46.0921890473
423 (in isoform 2)Ubiquitination-46.0921890473
425PhosphorylationTTIPTKQTQTFTTYS
CCCCCCEEEEEEEEC
31.0028152594
427PhosphorylationIPTKQTQTFTTYSDN
CCCCEEEEEEEECCC
26.7428152594
429PhosphorylationTKQTQTFTTYSDNQP
CCEEEEEEEECCCCC
28.3628152594
430O-linked_GlycosylationKQTQTFTTYSDNQPG
CEEEEEEEECCCCCE
19.4826374642
430PhosphorylationKQTQTFTTYSDNQPG
CEEEEEEEECCCCCE
19.4828152594
431PhosphorylationQTQTFTTYSDNQPGV
EEEEEEEECCCCCEE
15.8028152594
432PhosphorylationTQTFTTYSDNQPGVL
EEEEEEECCCCCEEE
28.1728152594
443PhosphorylationPGVLIQVYEGERAMT
CEEEEEEEECCCCCC
11.2228152594
450PhosphorylationYEGERAMTKDNNLLG
EECCCCCCCCCCCCC
33.9725849741
451AcetylationEGERAMTKDNNLLGK
ECCCCCCCCCCCCCE
45.4323749302
451MalonylationEGERAMTKDNNLLGK
ECCCCCCCCCCCCCE
45.4326320211
451UbiquitinationEGERAMTKDNNLLGK
ECCCCCCCCCCCCCE
45.4321890473
451 (in isoform 1)Ubiquitination-45.4321890473
451 (in isoform 2)Ubiquitination-45.4321890473
458UbiquitinationKDNNLLGKFELTGIP
CCCCCCCEEEEECCC
35.3221890473
458 (in isoform 1)Ubiquitination-35.3221890473
462PhosphorylationLLGKFELTGIPPAPR
CCCEEEEECCCCCCC
26.3526552605
469DimethylationTGIPPAPRGVPQIEV
ECCCCCCCCCCEEEE
61.93-
469MethylationTGIPPAPRGVPQIEV
ECCCCCCCCCCEEEE
61.9324129315
477PhosphorylationGVPQIEVTFDIDANG
CCCEEEEEEEECCCC
11.6422817900
495PhosphorylationVSAVDKSTGKENKIT
EEEEECCCCCCCCEE
59.00-
497AcetylationAVDKSTGKENKITIT
EEECCCCCCCCEEEE
59.1925953088
497UbiquitinationAVDKSTGKENKITIT
EEECCCCCCCCEEEE
59.19-
500AcetylationKSTGKENKITITNDK
CCCCCCCCEEEECCC
42.1725953088
500UbiquitinationKSTGKENKITITNDK
CCCCCCCCEEEECCC
42.1721906983
500 (in isoform 1)Ubiquitination-42.1721890473
502PhosphorylationTGKENKITITNDKGR
CCCCCCEEEECCCCC
24.2925159151
504PhosphorylationKENKITITNDKGRLS
CCCCEEEECCCCCCC
28.8123312004
507SumoylationKITITNDKGRLSKED
CEEEECCCCCCCHHH
48.26-
507AcetylationKITITNDKGRLSKED
CEEEECCCCCCCHHH
48.2623749302
507SuccinylationKITITNDKGRLSKED
CEEEECCCCCCCHHH
48.2623954790
507SumoylationKITITNDKGRLSKED
CEEEECCCCCCCHHH
48.26-
507UbiquitinationKITITNDKGRLSKED
CEEEECCCCCCCHHH
48.2621890473
507 (in isoform 1)Ubiquitination-48.2621890473
511PhosphorylationTNDKGRLSKEDIERM
ECCCCCCCHHHHHHH
32.4129255136
512AcetylationNDKGRLSKEDIERMV
CCCCCCCHHHHHHHH
65.0925825284
512MalonylationNDKGRLSKEDIERMV
CCCCCCCHHHHHHHH
65.0926320211
512SuccinylationNDKGRLSKEDIERMV
CCCCCCCHHHHHHHH
65.09-
512SuccinylationNDKGRLSKEDIERMV
CCCCCCCHHHHHHHH
65.09-
512SumoylationNDKGRLSKEDIERMV
CCCCCCCHHHHHHHH
65.0919608861
512UbiquitinationNDKGRLSKEDIERMV
CCCCCCCHHHHHHHH
65.0921890473
512 (in isoform 1)Ubiquitination-65.0921890473
524AcetylationRMVQEAEKYKAEDEK
HHHHHHHHHCHHCHH
60.1323749302
524UbiquitinationRMVQEAEKYKAEDEK
HHHHHHHHHCHHCHH
60.1319608861
524 (in isoform 1)Ubiquitination-60.1321890473
525PhosphorylationMVQEAEKYKAEDEKQ
HHHHHHHHCHHCHHH
13.61-
526AcetylationVQEAEKYKAEDEKQR
HHHHHHHCHHCHHHH
57.2625953088
526UbiquitinationVQEAEKYKAEDEKQR
HHHHHHHCHHCHHHH
57.2621906983
526 (in isoform 1)Ubiquitination-57.2621890473
531AcetylationKYKAEDEKQRDKVSS
HHCHHCHHHHHHCCC
64.0623749302
531UbiquitinationKYKAEDEKQRDKVSS
HHCHHCHHHHHHCCC
64.0621906983
531 (in isoform 1)Ubiquitination-64.0621890473
535UbiquitinationEDEKQRDKVSSKNSL
HCHHHHHHCCCCHHH
46.32-
537PhosphorylationEKQRDKVSSKNSLES
HHHHHHCCCCHHHHH
41.1423403867
538PhosphorylationKQRDKVSSKNSLESY
HHHHHCCCCHHHHHH
38.5523403867
539AcetylationQRDKVSSKNSLESYA
HHHHCCCCHHHHHHH
42.957925255
539UbiquitinationQRDKVSSKNSLESYA
HHHHCCCCHHHHHHH
42.9521890473
539 (in isoform 1)Ubiquitination-42.9521890473
541PhosphorylationDKVSSKNSLESYAFN
HHCCCCHHHHHHHHE
36.9323401153
544PhosphorylationSSKNSLESYAFNMKA
CCCHHHHHHHHEEEC
27.3625159151
545PhosphorylationSKNSLESYAFNMKAT
CCHHHHHHHHEEECE
13.0623403867
549SulfoxidationLESYAFNMKATVEDE
HHHHHHEEECEECCH
2.2321406390
550AcetylationESYAFNMKATVEDEK
HHHHHEEECEECCHH
41.8525953088
550UbiquitinationESYAFNMKATVEDEK
HHHHHEEECEECCHH
41.8521906983
550 (in isoform 1)Ubiquitination-41.8521890473
557"N6,N6-dimethyllysine"KATVEDEKLQGKIND
ECEECCHHHCCCCCH
59.43-
557AcetylationKATVEDEKLQGKIND
ECEECCHHHCCCCCH
59.4321466224
557MethylationKATVEDEKLQGKIND
ECEECCHHHCCCCCH
59.4324129315
557UbiquitinationKATVEDEKLQGKIND
ECEECCHHHCCCCCH
59.4321906983
557 (in isoform 1)Ubiquitination-59.4321890473
561"N6,N6,N6-trimethyllysine"EDEKLQGKINDEDKQ
CCHHHCCCCCHHHHH
25.94-
561AcetylationEDEKLQGKINDEDKQ
CCHHHCCCCCHHHHH
25.9421466224
561MethylationEDEKLQGKINDEDKQ
CCHHHCCCCCHHHHH
25.9423349634
561UbiquitinationEDEKLQGKINDEDKQ
CCHHHCCCCCHHHHH
25.9421906983
561 (in isoform 1)Ubiquitination-25.9421890473
567"N6,N6-dimethyllysine"GKINDEDKQKILDKC
CCCCHHHHHHHHHHH
51.98-
567AcetylationGKINDEDKQKILDKC
CCCCHHHHHHHHHHH
51.9821466224
567MethylationGKINDEDKQKILDKC
CCCCHHHHHHHHHHH
51.9823748837
569"N6,N6-dimethyllysine"INDEDKQKILDKCNE
CCHHHHHHHHHHHHH
51.48-
569AcetylationINDEDKQKILDKCNE
CCHHHHHHHHHHHHH
51.4821466224
569MethylationINDEDKQKILDKCNE
CCHHHHHHHHHHHHH
51.4823748837
573AcetylationDKQKILDKCNEIINW
HHHHHHHHHHHHHHH
35.2025953088
573UbiquitinationDKQKILDKCNEIINW
HHHHHHHHHHHHHHH
35.2021906983
573 (in isoform 1)Ubiquitination-35.2021890473
574S-nitrosocysteineKQKILDKCNEIINWL
HHHHHHHHHHHHHHH
5.73-
574GlutathionylationKQKILDKCNEIINWL
HHHHHHHHHHHHHHH
5.7322555962
574S-nitrosylationKQKILDKCNEIINWL
HHHHHHHHHHHHHHH
5.7322178444
583AcetylationEIINWLDKNQTAEKE
HHHHHHCCCCHHHHH
49.1123749302
583SumoylationEIINWLDKNQTAEKE
HHHHHHCCCCHHHHH
49.11-
583UbiquitinationEIINWLDKNQTAEKE
HHHHHHCCCCHHHHH
49.1121890473
583 (in isoform 1)Ubiquitination-49.1121890473
589AcetylationDKNQTAEKEEFEHQQ
CCCCHHHHHHHHHHH
61.1419608861
589UbiquitinationDKNQTAEKEEFEHQQ
CCCCHHHHHHHHHHH
61.1421906983
589 (in isoform 1)Ubiquitination-61.1421890473
597AcetylationEEFEHQQKELEKVCN
HHHHHHHHHHHHHHH
58.6619608861
597MalonylationEEFEHQQKELEKVCN
HHHHHHHHHHHHHHH
58.6626320211
597UbiquitinationEEFEHQQKELEKVCN
HHHHHHHHHHHHHHH
58.6621890473
597 (in isoform 1)Ubiquitination-58.6621890473
601AcetylationHQQKELEKVCNPIIT
HHHHHHHHHHHHHHH
65.7919608861
601MalonylationHQQKELEKVCNPIIT
HHHHHHHHHHHHHHH
65.7926320211
601MethylationHQQKELEKVCNPIIT
HHHHHHHHHHHHHHH
65.7919608861
601UbiquitinationHQQKELEKVCNPIIT
HHHHHHHHHHHHHHH
65.7921890473
601 (in isoform 1)Ubiquitination-65.7921890473
603S-nitrosocysteineQKELEKVCNPIITKL
HHHHHHHHHHHHHHH
8.10-
603GlutathionylationQKELEKVCNPIITKL
HHHHHHHHHHHHHHH
8.1022555962
603S-nitrosylationQKELEKVCNPIITKL
HHHHHHHHHHHHHHH
8.1022178444
603S-palmitoylationQKELEKVCNPIITKL
HHHHHHHHHHHHHHH
8.1029575903
608PhosphorylationKVCNPIITKLYQSAG
HHHHHHHHHHHHHCC
18.7321712546
609UbiquitinationVCNPIITKLYQSAGG
HHHHHHHHHHHHCCC
34.49-
611PhosphorylationNPIITKLYQSAGGMP
HHHHHHHHHHCCCCC
11.2818691976
613PhosphorylationIITKLYQSAGGMPGG
HHHHHHHHCCCCCCC
18.4821406692
633PhosphorylationPGGGAPPSGGASSGP
CCCCCCCCCCCCCCC
49.1227134283
637PhosphorylationAPPSGGASSGPTIEE
CCCCCCCCCCCCCCC
38.8219413330
638PhosphorylationPPSGGASSGPTIEEV
CCCCCCCCCCCCCCC
48.5419413330
641PhosphorylationGGASSGPTIEEVD--
CCCCCCCCCCCCC--
44.5427134283

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
-KUbiquitinationE3 ubiquitin ligaseSTUB1Q9UNE7
PMID:11146634

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
561KMethylation

23349634

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 HSP7C_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HPBP1_HUMANHSPBP1physical
16189514
NOA1_HUMANNOA1physical
16169070
T4S1_HUMANTM4SF1physical
16169070
ERH_HUMANERHphysical
16169070
F16P1_HUMANFBP1physical
16169070
UBC_HUMANUBCphysical
16169070
DNJA3_HUMANDNAJA3physical
11679576
HS90A_HUMANHSP90AA1physical
9269769
PP1A_HUMANPPP1CAphysical
9269769
MYPT2_HUMANPPP1R12Bphysical
9269769
BAG2_HUMANBAG2physical
9873016
BAG3_HUMANBAG3physical
9873016
BAG4_HUMANBAG4physical
11909948
TERA_HUMANVCPphysical
16621797
CCND1_HUMANCCND1physical
18537972
CDK4_HUMANCDK4physical
18537972
BAG1_HUMANBAG1physical
12297498
CFTR_HUMANCFTRphysical
10982807
CFTR_HUMANCFTRphysical
10666020
CHIP_HUMANSTUB1physical
21454478
CFTR_HUMANCFTRphysical
21697503
ERG_HUMANERGphysical
21183741
HD_HUMANHTTphysical
20026656
UBE3A_HUMANUBE3Aphysical
19233847
BCR_HUMANBCRphysical
20675402
ABL1_HUMANABL1physical
20675402
P53_HUMANTP53physical
8729618
BAG1_HUMANBAG1physical
11741305
CFTR_HUMANCFTRphysical
11146634
CAPZB_HUMANCAPZBphysical
20884878
CAZA1_HUMANCAPZA1physical
20884878
SYUA_HUMANSNCAphysical
22776201
TERA_HUMANVCPphysical
22939629
VAMP2_HUMANVAMP2physical
22939629
PRKDC_HUMANPRKDCphysical
22939629
RNPS1_HUMANRNPS1physical
22939629
PDIA3_HUMANPDIA3physical
22939629
ROA3_HUMANHNRNPA3physical
22939629
RS4X_HUMANRPS4Xphysical
22939629
SAM50_HUMANSAMM50physical
22939629
SC24C_HUMANSEC24Cphysical
22939629
STIP1_HUMANSTIP1physical
22939629
SSBP_HUMANSSBP1physical
22939629
RS15A_HUMANRPS15Aphysical
22939629
RL18A_HUMANRPL18Aphysical
22939629
NECP2_HUMANNECAP2physical
22939629
SON_HUMANSONphysical
22939629
RL8_HUMANRPL8physical
22939629
SC31A_HUMANSEC31Aphysical
22939629
PO2F1_HUMANPOU2F1physical
22939629
NAL12_HUMANNLRP12physical
17947705
MIPT3_HUMANTRAF3IP1physical
20391533
KCNQ4_HUMANKCNQ4physical
23431407
SRRT_HUMANSRRTphysical
22365833
CCAR2_HUMANCCAR2physical
22365833
BAG2_HUMANBAG2physical
22365833
CCND1_HUMANCCND1physical
23217712
BAG1_HUMANBAG1physical
19800331
RAF1_HUMANRAF1physical
16093354
ESR1_HUMANESR1physical
9774640
STIP1_HUMANSTIP1physical
9774640
DNJC7_HUMANDNAJC7physical
10567422
TTC1_HUMANTTC1physical
10567422
SGTA_HUMANSGTAphysical
10567422
STIP1_HUMANSTIP1physical
10567422
CHIP_HUMANSTUB1physical
23865999
STIP1_HUMANSTIP1physical
11093761
DNJB1_HUMANDNAJB1physical
11093761
F10A1_HUMANST13physical
11093761
TGM2_HUMANTGM2physical
21988832
SGTA_HUMANSGTAphysical
21988832
CFTR_HUMANCFTRphysical
23990462
TF65_HUMANRELAphysical
24175631
ASNA_HUMANASNA1physical
22863883
SYYC_HUMANYARSphysical
22863883
BAG2_HUMANBAG2physical
25036637
HS105_HUMANHSPH1physical
25036637
BAG3_HUMANBAG3physical
25036637
HSP72_HUMANHSPA2physical
25036637
BAG4_HUMANBAG4physical
25036637
DNJB6_HUMANDNAJB6physical
25036637
EDRF1_HUMANEDRF1physical
25036637
DNJC9_HUMANDNAJC9physical
25036637
GBRB1_HUMANGABRB1physical
25036637
HSP74_HUMANHSPA4physical
25036637
HS74L_HUMANHSPA4Lphysical
25036637
HPBP1_HUMANHSPBP1physical
25036637
HYOU1_HUMANHYOU1physical
25036637
TBA1A_HUMANTUBA1Aphysical
25036637
F10A1_HUMANST13physical
25036637
DNJA1_HUMANDNAJA1physical
25036637
CHIP_HUMANSTUB1physical
25036637
DJB12_HUMANDNAJB12physical
25036637
GCST_HUMANAMTphysical
25036637
DNJA2_HUMANDNAJA2physical
25036637
SC24C_HUMANSEC24Cphysical
25036637
FWCH2_HUMANFLYWCH2physical
25036637
CHIP_HUMANSTUB1physical
16275660
NMI_HUMANNMIphysical
25416956
BAG3_HUMANBAG3physical
25416956
TRI38_HUMANTRIM38physical
25416956
HPBP1_HUMANHSPBP1physical
25416956
BAG1_HUMANBAG1physical
25535373
NNRE_HUMANAPOA1BPphysical
26344197
BAG2_HUMANBAG2physical
26344197
DNJA4_HUMANDNAJA4physical
26344197
DNJB4_HUMANDNAJB4physical
26344197
DNJC1_HUMANDNAJC1physical
26344197
DJC13_HUMANDNAJC13physical
26344197
DNJC2_HUMANDNAJC2physical
26344197
DUT_HUMANDUTphysical
26344197
FPPS_HUMANFDPSphysical
26344197
G3P_HUMANGAPDHphysical
26344197
HNRPD_HUMANHNRNPDphysical
26344197
HSP74_HUMANHSPA4physical
26344197
HS74L_HUMANHSPA4Lphysical
26344197
HS105_HUMANHSPH1physical
26344197
IPO7_HUMANIPO7physical
26344197
LMNB1_HUMANLMNB1physical
26344197
NACAM_HUMANNACAphysical
26344197
NACA_HUMANNACAphysical
26344197
RL13A_HUMANRPL13Aphysical
26344197
RL7_HUMANRPL7physical
26344197
RS4X_HUMANRPS4Xphysical
26344197
STIP1_HUMANSTIP1physical
26344197
TBB5_HUMANTUBBphysical
26344197
RN207_HUMANRNF207physical
25281747
HIS3_HUMANHTN3physical
26775844
P53_HUMANTP53physical
7954368
HS90A_HUMANHSP90AA1physical
22504172
CLC4K_HUMANCD207physical
28514442
HSF1_HUMANHSF1physical
28514442
ABL2_HUMANABL2physical
28514442
EDRF1_HUMANEDRF1physical
28514442
DJC13_HUMANDNAJC13physical
28514442
GAK_HUMANGAKphysical
28514442
ARFP1_HUMANARFIP1physical
28514442
SF3A2_HUMANSF3A2physical
28514442
RPRD2_HUMANRPRD2physical
28514442
TBCE_HUMANTBCEphysical
28514442
HPBP1_HUMANHSPBP1physical
28514442
CF106_HUMANC6orf106physical
28514442
EP300_HUMANEP300physical
28514442
SRP54_HUMANSRP54physical
28514442
TACC3_HUMANTACC3physical
28514442
MARE2_HUMANMAPRE2physical
28514442
A1AT_HUMANSERPINA1physical
28514442
HSP72_HUMANHSPA2physical
28514442
ZN703_HUMANZNF703physical
28514442
KCD15_HUMANKCTD15physical
28514442
HBB_HUMANHBBphysical
28514442
SF3A3_HUMANSF3A3physical
28514442
TAU_HUMANMAPTphysical
28514442
VIGLN_HUMANHDLBPphysical
28514442
H15_HUMANHIST1H1Bphysical
28514442
NFS1_HUMANNFS1physical
28514442
MP2K2_HUMANMAP2K2physical
28514442
QRIC1_HUMANQRICH1physical
28514442
TAB1_HUMANTAB1physical
28514442
WNK1_HUMANWNK1physical
28514442
NUCG_HUMANENDOGphysical
28514442
CKAP5_HUMANCKAP5physical
28514442
GANAB_HUMANGANABphysical
28514442
PP1R8_HUMANPPP1R8physical
28514442
MAVS_HUMANMAVSphysical
28514442
RNF25_HUMANRNF25physical
28514442
MD1L1_HUMANMAD1L1physical
28514442
FOXC1_HUMANFOXC1physical
28514442
ATF1_HUMANATF1physical
28514442
CSTF3_HUMANCSTF3physical
28514442
ALBU_HUMANALBphysical
28514442
NB5R3_HUMANCYB5R3physical
28514442
CSDE1_HUMANCSDE1physical
28514442
GLIP1_HUMANGLIPR1physical
23333597
SP1_HUMANSP1physical
23333597
MYB_HUMANMYBphysical
23333597
FANCA_HUMANFANCAphysical
28215707
P53_HUMANTP53physical
28215707
BAG1_HUMANBAG1physical
28215707
SODC_HUMANSOD1physical
28215707
LAMP2_HUMANLAMP2physical
28465257
EP300_HUMANEP300physical
28465257
CBP_HUMANCREBBPphysical
28465257
UBQL2_HUMANUBQLN2physical
27477512

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 HSP7C_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-88; LYS-108; LYS-246;LYS-319; LYS-348; LYS-512; LYS-524; LYS-589; LYS-597 AND LYS-601, ANDMASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-541; SER-637 ANDSER-638, AND MASS SPECTROMETRY.
"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-113; TYR-115; SER-120AND SER-121, AND MASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-477, AND MASSSPECTROMETRY.
"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-41 AND TYR-107, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15, AND MASSSPECTROMETRY.

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