Overview
| Uniprot ID | P34931 |
|---|
| Protein Name | Heat shock 70 kDa protein 1-like |
|---|
| Gene Name | HSPA1L |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 104 |
INEGGKPKVLVSYKG |
Function
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). Positive regulator of PRKN translocation to damaged mitochondria (PubMed:24270810)
Protein Sequence
10
MATAKGIAIG
20
IDLGTTYSCV
30
GVFQHGKVEI
40
IANDQGNRTT
50
PSYVAFTDTE
60
RLIGDAAKNQ
70
VAMNPQNTVF
80
DAKRLIGRKF
90
NDPVVQADMK
100
LWPFQVINEG
110
GKPKVLVSYK
120
GENKAFYPEE
130
ISSMVLTKLK
140
ETAEAFLGHP
150
VTNAVITVPA
160
YFNDSQRQAT
170
KDAGVIAGLN
180
VLRIINEPTA
190
AAIAYGLDKG
200
GQGERHVLIF
210
DLGGGTFDVS
220
ILTIDDGIFE
230
VKATAGDTHL
240
GGEDFDNRLV
250
SHFVEEFKRK
260
HKKDISQNKR
270
AVRRLRTACE
280
RAKRTLSSST
290
QANLEIDSLY
300
EGIDFYTSIT
310
RARFEELCAD
320
LFRGTLEPVE
330
KALRDAKMDK
340
AKIHDIVLVG
350
GSTRIPKVQR
360
LLQDYFNGRD
370
LNKSINPDEA
380
VAYGAAVQAA
390
ILMGDKSEKV
400
QDLLLLDVAP
410
LSLGLETAGG
420
VMTALIKRNS
430
TIPTKQTQIF
440
TTYSDNQPGV
450
LIQVYEGERA
460
MTKDNNLLGR
470
FDLTGIPPAP
480
RGVPQIEVTF
490
DIDANGILNV
500
TATDKSTGKV
510
NKITITNDKG
520
RLSKEEIERM
530
VLDAEKYKAE
540
DEVQREKIAA
550
KNALESYAFN
560
MKSVVSDEGL
570
KGKISESDKN
580
KILDKCNELL
590
SWLEVNQLAE
600
KDEFDHKRKE
610
LEQMCNPIIT
620
KLYQGGCTGP
630
ACGTGYVPGR
640
PATGPTIEEV
D
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0072562 |
blood microparticle |
| Cellular Component |
GO:0044297 |
cell body |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0005886 |
plasma membrane |
| Cellular Component |
GO:0002199 |
zona pellucida receptor complex |
| Molecular Function |
GO:0005524 |
ATP binding |
| Molecular Function |
GO:0016887 |
ATP hydrolysis activity |
| Molecular Function |
GO:0031072 |
heat shock protein binding |
| Molecular Function |
GO:0044183 |
protein folding chaperone |
| Molecular Function |
GO:0031625 |
ubiquitin protein ligase binding |
| Molecular Function |
GO:0051082 |
unfolded protein binding |
| Biological Process |
GO:1903955 |
positive regulation of protein targeting to mitochondrion |
| Biological Process |
GO:0042026 |
protein refolding |
| Biological Process |
GO:0006986 |
response to unfolded protein |
Reference
[1] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.