产品描述
*The optimal dilutions should be determined by the end user.
*Tips:
WB: 适用于变性蛋白样本的免疫印迹检测. IHC: 适用于组织样本的石蜡(IHC-p)或冰冻(IHC-f)切片样本的免疫组化/荧光检测. IF/ICC: 适用于细胞样本的荧光检测. ELISA(peptide): 适用于抗原肽的ELISA检测.
展开/折叠
60 kDa chaperonin; 60 kDa heat shock protein, mitochondrial; CH60_HUMAN; Chaperonin 60; Chaperonin, 60-KD; CPN60; fa04a05; GROEL; heat shock 60kDa protein 1 (chaperonin); Heat shock protein 1 (chaperonin); Heat shock protein 60; Heat shock protein 65; heat shock protein family D (Hsp60) member 1; HLD4; Hsp 60; HSP 65; HSP-60; HSP60; HSP65; HSPD1; HuCHA60; Mitochondrial matrix protein P1; P60 lymphocyte protein; short heat shock protein 60 Hsp60s1; SPG13;
抗原和靶标
A synthesized peptide derived from human HSP60.
- P10809 CH60_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MLRLPTVFRQMRPVSRVLAPHLTRAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEGLTLNLEDVQPHDLGKVGEVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALNATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSEVGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKEEKDPGMGAMGGMGGGMGGGMF
翻译修饰 - P10809 作为底物
| Site | PTM Type | Enzyme | Source |
|---|---|---|---|
| R3 | Methylation | Uniprot | |
| K31 | Acetylation | Uniprot | |
| K31 | Ubiquitination | Uniprot | |
| K58 | Ubiquitination | Uniprot | |
| T61 | Phosphorylation | Uniprot | |
| S67 | Phosphorylation | Uniprot | |
| S70 | Phosphorylation | Uniprot | |
| K72 | Ubiquitination | Uniprot | |
| T74 | Phosphorylation | Uniprot | |
| K75 | Ubiquitination | Uniprot | |
| T79 | Phosphorylation | Uniprot | |
| K82 | Acetylation | Uniprot | |
| K82 | Ubiquitination | Uniprot | |
| S83 | Phosphorylation | Uniprot | |
| K87 | Acetylation | Uniprot | |
| K87 | Ubiquitination | Uniprot | |
| Y90 | Phosphorylation | Uniprot | |
| K91 | Acetylation | Uniprot | |
| K91 | Ubiquitination | Uniprot | |
| K96 | Acetylation | Uniprot | |
| K96 | Ubiquitination | Uniprot | |
| T105 | Phosphorylation | Uniprot | |
| T113 | Phosphorylation | Uniprot | |
| T114 | Phosphorylation | Uniprot | |
| T115 | Phosphorylation | Uniprot | |
| K125 | Acetylation | Uniprot | |
| K125 | Ubiquitination | Uniprot | |
| K130 | Acetylation | Uniprot | |
| K130 | Ubiquitination | Uniprot | |
| S132 | Phosphorylation | Uniprot | |
| K133 | Acetylation | Uniprot | |
| K133 | Ubiquitination | Uniprot | |
| R141 | Methylation | Uniprot | |
| K156 | Acetylation | Uniprot | |
| K157 | Acetylation | Uniprot | |
| S159 | Phosphorylation | Uniprot | |
| K160 | Ubiquitination | Uniprot | |
| T164 | Phosphorylation | Uniprot | |
| K180 | Acetylation | Uniprot | |
| S187 | Phosphorylation | Uniprot | |
| K191 | Acetylation | Uniprot | |
| K191 | Ubiquitination | Uniprot | |
| K192 | Acetylation | Uniprot | |
| K196 | Ubiquitination | Uniprot | |
| T200 | Phosphorylation | Uniprot | |
| K202 | Acetylation | Uniprot | |
| K202 | Ubiquitination | Uniprot | |
| T206 | Phosphorylation | Uniprot | |
| K218 | Acetylation | Uniprot | |
| K218 | Ubiquitination | Uniprot | |
| R221 | Methylation | Uniprot | |
| Y223 | Phosphorylation | Uniprot | |
| S225 | Phosphorylation | Uniprot | |
| Y227 | Phosphorylation | Uniprot | |
| T231 | Phosphorylation | Uniprot | |
| S232 | Phosphorylation | Uniprot | |
| K233 | Acetylation | Uniprot | |
| K233 | Ubiquitination | Uniprot | |
| K236 | Acetylation | Uniprot | |
| K236 | Ubiquitination | Uniprot | |
| C237 | S-Nitrosylation | Uniprot | |
| Y243 | Phosphorylation | Uniprot | |
| S247 | Phosphorylation | Uniprot | |
| K249 | Acetylation | Uniprot | |
| K249 | Ubiquitination | Uniprot | |
| K250 | Ubiquitination | Uniprot | |
| S252 | Phosphorylation | Uniprot | |
| S253 | Phosphorylation | Uniprot | |
| S256 | Phosphorylation | Uniprot | |
| K269 | Acetylation | Uniprot | |
| K292 | Methylation | Uniprot | |
| K292 | Ubiquitination | Uniprot | |
| K301 | Ubiquitination | Uniprot | |
| K352 | Acetylation | Uniprot | |
| K352 | Ubiquitination | Uniprot | |
| K359 | Acetylation | Uniprot | |
| K359 | Ubiquitination | Uniprot | |
| K364 | Acetylation | Uniprot | |
| K369 | Acetylation | Uniprot | |
| K369 | Ubiquitination | Uniprot | |
| T381 | Phosphorylation | Uniprot | |
| T382 | Phosphorylation | Uniprot | |
| S383 | Phosphorylation | Uniprot | |
| Y385 | Phosphorylation | Uniprot | |
| K387 | Acetylation | Uniprot | |
| K389 | Acetylation | Uniprot | |
| K396 | Acetylation | Uniprot | |
| K396 | Ubiquitination | Uniprot | |
| S398 | Phosphorylation | Uniprot | |
| T409 | Phosphorylation | Uniprot | |
| S410 | Phosphorylation | Uniprot | |
| K417 | Acetylation | Uniprot | |
| K417 | Ubiquitination | Uniprot | |
| T422 | Phosphorylation | Uniprot | |
| T428 | Phosphorylation | Uniprot | |
| C442 | S-Nitrosylation | Uniprot | |
| C447 | S-Nitrosylation | Uniprot | |
| T455 | Phosphorylation | Uniprot | |
| K462 | Acetylation | Uniprot | |
| K469 | Acetylation | Uniprot | |
| K469 | Ubiquitination | Uniprot | |
| T471 | Phosphorylation | Uniprot | |
| K473 | Acetylation | Uniprot | |
| K473 | Ubiquitination | Uniprot | |
| T478 | Phosphorylation | Uniprot | |
| K481 | Ubiquitination | Uniprot | |
| S488 | Phosphorylation | Uniprot | |
| S498 | Phosphorylation | Uniprot | |
| S499 | Phosphorylation | Uniprot | |
| Y503 | Phosphorylation | Uniprot | |
| K516 | Acetylation | Uniprot | |
| K516 | Methylation | Uniprot | |
| K516 | Ubiquitination | Uniprot | |
| T522 | Phosphorylation | Uniprot | |
| K523 | Acetylation | Uniprot | |
| K523 | Ubiquitination | Uniprot | |
| T527 | Phosphorylation | Uniprot | |
| T540 | Phosphorylation | Uniprot | |
| K551 | Acetylation | Uniprot |
研究背景
Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable).
Mitochondrion matrix.
Homoheptamer arranged in a ring structure. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. Interacts with 2 heptameric Hsp10 rings to form the symmetrical football complex. Interacts with HRAS (By similarity). Interacts with ATAD3A. Interacts with ETFBKMT and METTL21B. Interacts with MFHAS1.
(Microbial infection) Interacts with hepatits B virus/HBV protein X.
(Microbial infection) Interacts with HTLV-1 protein p40tax.
Belongs to the chaperonin (HSP60) family.
研究领域
· Genetic Information Processing > Folding, sorting and degradation > RNA degradation.
· Human Diseases > Endocrine and metabolic diseases > Type I diabetes mellitus.
· Human Diseases > Infectious diseases: Bacterial > Legionellosis.
· Human Diseases > Infectious diseases: Bacterial > Tuberculosis.
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